6RQQ

X-ray crystal structure of protiated (H) large 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
C	0004089	molecular_function	carbonate dehydratase activity
C	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	HOH540

---

site_id	AC2
Number of Residues	6
Details	binding site for residue FMT A 402

Chain	Residue
A	HOH540
A	HOH555
A	HIS226
A	HIS251
A	THR332
A	ZN401

---

site_id	AC3
Number of Residues	5
Details	binding site for residue ZN C 401

Chain	Residue
C	HIS226
C	HIS228
C	HIS251
C	FMT402
C	HOH528

---

site_id	AC4
Number of Residues	6
Details	binding site for residue FMT C 402

Chain	Residue
C	HIS226
C	HIS251
C	THR332
C	ZN401
C	HOH528
C	HOH580

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	HIS200
C	HIS200

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:19805286

Chain	Residue	Details
A	HIS226
A	HIS228
A	HIS251
C	HIS226
C	HIS228
C	HIS251

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	THR332
C	THR332

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18703501, ECO:0000269|PubMed:19805286

Chain	Residue	Details
A	ASN346
C	ASN346

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