4YGF

Crystal structure of the complex of Helicobacter pylori alpha-Carbonic Anhydrase with acetazolamide

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	d4ygfa_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	automated matches	automated matches	(Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
B	d4ygfb_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	automated matches	automated matches	(Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
C	d4ygfc_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	automated matches	automated matches	(Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
D	d4ygfd_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	automated matches	automated matches	(Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
E	d4ygfe_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	automated matches	automated matches	(Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
F	d4ygff_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	automated matches	automated matches	(Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
G	d4ygfg_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	automated matches	automated matches	(Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)
H	d4ygfh_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	automated matches	automated matches	(Helicobacter pylori 26695 ) [TaxId: 85962 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Carbonic anhydrase	8065137	3001672	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Carbonic anhydrase	8065137	3001672	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Carbonic anhydrase	8065137	3001672	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Carbonic anhydrase	8065137	3001672	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Carbonic anhydrase	8065137	3001672	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Carbonic anhydrase	8065137	3001672	SCOP2B (2022-06-29)
G	SCOP2 Family	Carbonic anhydrase	8065136	4002732	SCOP2 (2022-06-29)
G	SCOP2 Superfamily	Carbonic anhydrase	8065137	3001672	SCOP2 (2022-06-29)
H	SCOP2B Superfamily	Carbonic anhydrase	8065137	3001672	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	PF00194	e4ygfA1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: PF00194	ECOD (1.6)
B	PF00194	e4ygfB1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: PF00194	ECOD (1.6)
C	PF00194	e4ygfC1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: PF00194	ECOD (1.6)
D	PF00194	e4ygfD1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: PF00194	ECOD (1.6)
E	PF00194	e4ygfE1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: PF00194	ECOD (1.6)
F	PF00194	e4ygfF1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: PF00194	ECOD (1.6)
G	PF00194	e4ygfG1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: PF00194	ECOD (1.6)
H	PF00194	e4ygfH1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: PF00194	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)
B	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)
C	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)
D	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)
E	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)
F	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)
G	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)
H	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF00194	Eukaryotic-type carbonic anhydrase (Carb_anhydrase)	Eukaryotic-type carbonic anhydrase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	Alpha-carbonic anhydrase	cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding carbonate dehydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR041891	Carbonic anhydrase, prokaryotic-like	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR001148	Alpha carbonic anhydrase domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036398	Alpha carbonic anhydrase domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR023561	Carbonic anhydrase, alpha-class	Family

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.