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1URT

MURINE CARBONIC ANHYDRASE V

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 280
ChainResidue
AHIS94
AHIS96
AHIS119
AHOH281

site_idZIN
Number of Residues1
DetailsCATALYTICALLY ACTIVE METAL ION.
ChainResidue
AZN280

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHaVdghtYpaELHLV
ChainResidueDetails
ASER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11851394","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7479916","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8794740","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR199
AHIS64

246905

PDB entries from 2025-12-31

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