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

---

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

---

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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	257
Details	Domain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	Binding site: {"description":"in variant Michigan-1","evidences":[{"source":"PubMed","id":"12009884","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12009884","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16506782","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16870440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17314045","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17407288","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6430186","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7932756","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"804171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8057362","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8057362","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

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

---