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3DA2

X-ray structure of human carbonic anhydrase 13 in complex with inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0043209cellular_componentmyelin sheath
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0043209cellular_componentmyelin sheath
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS95
AHIS97
AHIS120

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS95
BHIS97
BHIS120

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL B 302
ChainResidue
BARG90

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 303
ChainResidue
BALA259
BPHE261

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 4MD A 401
ChainResidue
AGLN93
AHIS95
AHIS97
AHIS120
APHE132
AALA136
AHIS137
ALEU199
ATHR200

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 4MD B 401
ChainResidue
BGLN93
BHIS95
BHIS97
BHIS120
BPHE132
BALA136
BHIS137
BLEU199
BTHR200
BPRO203
BTRP210

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHiVdgvsYaaELHVV
ChainResidueDetails
ASER106-VAL122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues257
DetailsDomain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18618712","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR200
AHIS65

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
BTHR200
BHIS65

239803

PDB entries from 2025-08-06

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