1HCB

ENZYME-SUBSTRATE INTERACTIONS: STRUCTURE OF HUMAN CARBONIC ANHYDRASE I COMPLEXED WITH BICARBONATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004064	molecular_function	arylesterase activity
A	0004089	molecular_function	carbonate dehydratase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0009750	biological_process	response to fructose
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0018820	molecular_function	cyanamide hydratase activity
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 261

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	HOH520
A	HOH521
A	BCT522

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site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BCT A 522

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	LEU198
A	THR199
A	TRP209
A	ZN261
A	HOH361
A	HOH520
A	HOH521

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site_id	CAT
Number of Residues	10
Details	CATALYTIC ACTIVE SITE OF THE ENZYME. SUBSTRATE BICARBONATE ANION BINDS IN THE POCKET DEFINED BY THESE RESIDUES AND IS A DONOR OF A H-BOND TO OG1 THR 199

Chain	Residue
A	HIS94
A	ZN261
A	HIS96
A	HIS119
A	ALA121
A	VAL143
A	LEU198
A	THR199
A	VAL207
A	TRP209

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Functional Information from PROSITE/UniProt

site_id	PS00162
Number of Residues	17
Details	ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYsaELHVA

Chain	Residue	Details
A	SER105-ALA121

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	SER65

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: in variant Michigan-1 => ECO:0000269|PubMed:12009884

Chain	Residue	Details
A	SER65
A	VAL68
A	PRO201

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362

Chain	Residue	Details
A	PHE95
A	TRP97
A	VAL120

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:8057362

Chain	Residue	Details
A	HIS200

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000269|PubMed:4207120, ECO:0000269|PubMed:4217196

Chain	Residue	Details
A	SER2

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ca2

Chain	Residue	Details
A	THR199
A	HIS64

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