1RWI

Extracellular domain of Mycobacterium tuberculosis PknD

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 [auth B]	d1rwib1	All beta proteins	6-bladed beta-propeller	NHL repeat	NHL repeat	Serine/threonine-protein kinase PknD	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
A [auth B]	d1rwib2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
B [auth A]	d1rwia1	All beta proteins	6-bladed beta-propeller	NHL repeat	NHL repeat	Serine/threonine-protein kinase PknD	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
B [auth A]	d1rwia2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth B]	SCOP2B Superfamily	NHL repeat-like	8041045	3000174	SCOP2B (2022-06-29)
B [auth A]	SCOP2 Family	NHL repeat-like	8028666	4000932	SCOP2 (2022-06-29)
B [auth A]	SCOP2 Superfamily	NHL repeat-like	8041045	3000174	SCOP2 (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 [auth B]	PF01436	e1rwiB1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 6-bladed	F: PF01436	ECOD (1.6)
B [auth A]	PF01436	e1rwiA1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 6-bladed	F: PF01436	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	2.120.10.30	Mainly Beta	6 Propeller	Neuraminidase	TolB, C-terminal domain	CATH (4.3.0)
B [auth A]	2.120.10.30	Mainly Beta	6 Propeller	Neuraminidase	TolB, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A]	PF01436	NHL repeat (NHL)	NHL repeat	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A]	Serine/threonine-protein kinase pknD	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding catalytic activity, acting on a protein kinase activity protein kinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups protein serine/threonine kinase activity cation binding manganese ion binding transition metal ion binding metal ion binding protein serine kinase activity	regulation of molecular function regulation of catalytic activity biological regulation negative regulation of molecular function negative regulation of catalytic activity regulation of protein binding negative regulation of protein binding negative regulation of binding regulation of binding phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process regulation of molecular function regulation of catalytic activity biological regulation negative regulation of molecular function negative regulation of catalytic activity regulation of protein binding negative regulation of protein binding negative regulation of binding regulation of binding phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process positive regulation of molecular function positive regulation of catalytic activity regulation of cellular process negative regulation of small molecule metabolic process oxoacid metabolic process regulation of lipid metabolic process negative regulation of biological process organic acid metabolic process organic acid biosynthetic process negative regulation of lipid biosynthetic process negative regulation of cellular metabolic process carboxylic acid biosynthetic process regulation of primary metabolic process cellular ketone metabolic process regulation of small molecule metabolic process organic substance biosynthetic process small molecule metabolic process regulation of biological process regulation of cellular ketone metabolic process negative regulation of metabolic process regulation of cellular metabolic process primary metabolic process negative regulation of cellular biosynthetic process biosynthetic process cellular lipid metabolic process regulation of fatty acid metabolic process regulation of fatty acid biosynthetic process monocarboxylic acid metabolic process regulation of metabolic process negative regulation of lipid metabolic process cellular biosynthetic process lipid biosynthetic process organic substance metabolic process negative regulation of cellular process negative regulation of fatty acid biosynthetic process regulation of biosynthetic process fatty acid metabolic process negative regulation of fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process carboxylic acid metabolic process fatty acid biosynthetic process regulation of cellular biosynthetic process negative regulation of biosynthetic process regulation of lipid biosynthetic process lipid metabolic process cellular response to stimulus cellular response to nutrient levels response to nutrient levels cellular response to phosphate starvation response to stimulus cellular response to stress response to stress response to starvation cellular response to starvation	extracellular region cellular anatomical entity intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane external encapsulating structure cell wall peptidoglycan-based cell wall

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A]	IPR011042	Six-bladed beta-propeller, TolB-like	Homologous Superfamily
A [auth B], B [auth A]	IPR017441	Protein kinase, ATP binding site	Binding Site
A [auth B], B [auth A]	IPR001258	NHL repeat	Repeat
A [auth B], B [auth A]	IPR011009	Protein kinase-like domain superfamily	Homologous Superfamily
A [auth B], B [auth A]	IPR035016	Protein kinase PknD, NHL repeat domain	Domain
A [auth B], B [auth A]	IPR000719	Protein kinase domain	Domain
A [auth B], B [auth A]	IPR008271	Serine/threonine-protein kinase, active site	Active Site

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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.