6RQW

X-ray crystal structure of perdeuterated (D) small monoclinic unit cell CA IX SV.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0008270	molecular_function	zinc ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue ZN A 401

Chain	Residue
A	HIS226
A	HIS228
A	HIS251
A	FMT402
A	HOH508

---

site_id	AC2
Number of Residues	7
Details	binding site for residue FMT A 402

Chain	Residue
A	ZN401
A	HOH508
A	HOH553
A	HIS226
A	HIS251
A	LEU331
A	THR332

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER237-VAL253

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19805286","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18703501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19805286","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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