1RP5

PBP2x from Streptococcus pneumoniae strain 5259 with reduced susceptibility to beta-lactam antibiotics

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1rp5a1	Alpha and beta proteins (a+b)	Penicillin-binding protein 2x (pbp-2x), c-terminal domain	Penicillin-binding protein 2x (pbp-2x), c-terminal domain	Penicillin-binding protein 2x (pbp-2x), c-terminal domain	Penicillin-binding protein 2x (pbp-2x), c-terminal domain	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
A	d1rp5a3	Alpha and beta proteins (a+b)	Penicillin binding protein dimerisation domain	Penicillin binding protein dimerisation domain	Penicillin binding protein dimerisation domain	Penicillin-binding protein 2x (pbp-2x), N-terminal domain	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
A	d1rp5a4	Multi-domain proteins (alpha and beta)	beta-lactamase/transpeptidase-like	beta-lactamase/transpeptidase-like	beta-Lactamase/D-ala carboxypeptidase	Penicillin-binding protein 2x (pbp-2x), transpeptidase domain	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
B	d1rp5b1	Alpha and beta proteins (a+b)	Penicillin-binding protein 2x (pbp-2x), c-terminal domain	Penicillin-binding protein 2x (pbp-2x), c-terminal domain	Penicillin-binding protein 2x (pbp-2x), c-terminal domain	Penicillin-binding protein 2x (pbp-2x), c-terminal domain	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
B	d1rp5b3	Alpha and beta proteins (a+b)	Penicillin binding protein dimerisation domain	Penicillin binding protein dimerisation domain	Penicillin binding protein dimerisation domain	Penicillin-binding protein 2x (pbp-2x), N-terminal domain	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)
B	d1rp5b4	Multi-domain proteins (alpha and beta)	beta-lactamase/transpeptidase-like	beta-lactamase/transpeptidase-like	beta-Lactamase/D-ala carboxypeptidase	Penicillin-binding protein 2x (pbp-2x), transpeptidase domain	(Streptococcus pneumoniae ) [TaxId: 1313 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Penicillin binding protein dimerisation domain	8037247	3001420	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Penicillin-binding protein 2x (pbp-2x) c-terminal domain	8034366	3000202	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Penicillin-binding protein 2x (pbp-2x) c-terminal domain	8034369	3000202	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	beta-lactamase/transpeptidase-like	8037377	3001604	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Penicillin binding protein dimerisation domain	8037247	3001420	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Penicillin-binding protein 2x (pbp-2x) c-terminal domain	8034366	3000202	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	beta-lactamase/transpeptidase-like	8037377	3001604	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Penicillin-binding protein 2x (pbp-2x) c-terminal domain	8034369	3000202	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PBP_dimer	e1rp5A6	A: beta complex topology	X: Penicillin binding protein dimerisation domain (From Topology)	H: Penicillin binding protein dimerisation domain (From Topology)	T: Penicillin binding protein dimerisation domain	F: PBP_dimer	ECOD (1.6)
A	PASTA_2	e1rp5A4	A: a+b two layers	X: CI-2 family of serine protease inhibitors-like	H: Penicillin-binding protein 2x (pbp-2x)-C (From Topology)	T: Penicillin-binding protein 2x (pbp-2x)-C	F: PASTA_2	ECOD (1.6)
A	PASTA_1	e1rp5A8	A: a+b two layers	X: CI-2 family of serine protease inhibitors-like	H: Penicillin-binding protein 2x (pbp-2x)-C (From Topology)	T: Penicillin-binding protein 2x (pbp-2x)-C	F: PASTA_1	ECOD (1.6)
A	PBP_2x_ClpS	e1rp5A7	A: a+b two layers	X: ClpS-like	H: Penicillin binding protein ClpS-like domain (From Topology)	T: Penicillin binding protein ClpS-like domain	F: PBP_2x_ClpS	ECOD (1.6)
A	Transpeptidase_1st_1	e1rp5A5	A: a+b three layers	X: Profilin-like	H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: a+b domain in beta-lactamase/transpeptidase-like proteins	F: Transpeptidase_1st_1	ECOD (1.6)
B	PBP_dimer	e1rp5B2	A: beta complex topology	X: Penicillin binding protein dimerisation domain (From Topology)	H: Penicillin binding protein dimerisation domain (From Topology)	T: Penicillin binding protein dimerisation domain	F: PBP_dimer	ECOD (1.6)
B	PASTA_2	e1rp5B4	A: a+b two layers	X: CI-2 family of serine protease inhibitors-like	H: Penicillin-binding protein 2x (pbp-2x)-C (From Topology)	T: Penicillin-binding protein 2x (pbp-2x)-C	F: PASTA_2	ECOD (1.6)
B	PASTA_1	e1rp5B6	A: a+b two layers	X: CI-2 family of serine protease inhibitors-like	H: Penicillin-binding protein 2x (pbp-2x)-C (From Topology)	T: Penicillin-binding protein 2x (pbp-2x)-C	F: PASTA_1	ECOD (1.6)
B	PBP_2x_ClpS	e1rp5B1	A: a+b two layers	X: ClpS-like	H: Penicillin binding protein ClpS-like domain (From Topology)	T: Penicillin binding protein ClpS-like domain	F: PBP_2x_ClpS	ECOD (1.6)
B	Transpeptidase_1st_1	e1rp5B5	A: a+b three layers	X: Profilin-like	H: a+b domain in beta-lactamase/transpeptidase-like proteins (From Topology)	T: a+b domain in beta-lactamase/transpeptidase-like proteins	F: Transpeptidase_1st_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.20.70.70	Mainly Beta	Single Sheet	Ubiquitin Ligase Nedd4	Chain: W	CATH (4.3.0)
A	3.90.1310.10	Alpha Beta	Alpha-Beta Complex	Penicillin-binding protein 2a (Domain 2)	Penicillin-binding protein 2a (Domain 2)	CATH (4.3.0)
A	3.30.70.2110	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
A	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)
B	2.20.70.70	Mainly Beta	Single Sheet	Ubiquitin Ligase Nedd4	Chain: W	CATH (4.3.0)
B	3.90.1310.10	Alpha Beta	Alpha-Beta Complex	Penicillin-binding protein 2a (Domain 2)	Penicillin-binding protein 2a (Domain 2)	CATH (4.3.0)
B	3.30.70.2110	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
B	3.40.710.10	Alpha Beta	3-Layer(aba) Sandwich	Beta-lactamase	DD-peptidase/beta-lactamase superfamily	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03717	Penicillin-binding Protein dimerisation domain (PBP_dimer)	Penicillin-binding Protein dimerisation domain	This domain is found at the N terminus of Class B High Molecular Weight Penicillin-Binding Proteins. Its function has not been precisely defined, but is strongly implicated in PBP polymerisation. The domain forms a largely disordered 'sugar tongs' st ...	This domain is found at the N terminus of Class B High Molecular Weight Penicillin-Binding Proteins. Its function has not been precisely defined, but is strongly implicated in PBP polymerisation. The domain forms a largely disordered 'sugar tongs' structure.	Domain
A, B	PF00905	Penicillin binding protein transpeptidase domain (Transpeptidase)	Penicillin binding protein transpeptidase domain	The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family.	Domain
A, B	PF03793	PASTA domain (PASTA)	PASTA domain	This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases [1]. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a smal ...	This domain is found at the C termini of several Penicillin-binding proteins and bacterial serine/threonine kinases [1]. It binds the beta-lactam stem, which implicates it in sensing D-alanyl-D-alanine - the PBP transpeptidase substrate. It is a small globular fold consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	penicillin-binding protein 2x	amide binding organic acid binding binding ion binding organic cyclic compound binding anion binding penicillin binding carboxylic acid binding heterocyclic compound binding monocarboxylic acid binding small molecule binding sulfur compound binding	developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis cellular process cell cycle cell division developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis cellular process cell cycle cell division cellular component organization cell wall organization or biogenesis cell wall organization cellular component organization or biogenesis external encapsulating structure organization response to stimulus response to chemical response to antibiotic cellular biosynthetic process glycosaminoglycan metabolic process organonitrogen compound biosynthetic process carbohydrate derivative metabolic process cellular component biogenesis organic substance metabolic process peptidoglycan metabolic process organic substance biosynthetic process glycosaminoglycan biosynthetic process carbohydrate derivative biosynthetic process peptidoglycan-based cell wall biogenesis organonitrogen compound metabolic process cellular metabolic process macromolecule biosynthetic process peptidoglycan biosynthetic process cell wall biogenesis biosynthetic process cell wall macromolecule biosynthetic process aminoglycan metabolic process aminoglycan biosynthetic process metabolic process macromolecule metabolic process	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR012338	Beta-lactamase/transpeptidase-like	Homologous Superfamily
A, B	IPR036138	Penicillin-binding protein, dimerisation domain superfamily	Homologous Superfamily
A, B	IPR005543	PASTA domain	Domain
A, B	IPR005311	Penicillin-binding protein, dimerisation domain	Domain
A, B	IPR001460	Penicillin-binding protein, transpeptidase	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.