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6RQQ

X-ray crystal structure of protiated (H) large monoclinic unit cell CA IX SV.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
C0004089molecular_functioncarbonate dehydratase activity
C0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
AHIS226
AHIS228
AHIS251
AFMT402
AHOH540

site_idAC2
Number of Residues6
Detailsbinding site for residue FMT A 402
ChainResidue
AHOH540
AHOH555
AHIS226
AHIS251
ATHR332
AZN401

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN C 401
ChainResidue
CHIS226
CHIS228
CHIS251
CFMT402
CHOH528

site_idAC4
Number of Residues6
Detailsbinding site for residue FMT C 402
ChainResidue
CHIS226
CHIS251
CTHR332
CZN401
CHOH528
CHOH580

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVeghrFpaEIHVV
ChainResidueDetails
ASER237-VAL253

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19805286","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18703501","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19805286","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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