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3D0N

Crystal structure of human carbonic anhydrase XIII

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
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
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AHIS94
AHIS96
AHIS119
ATHR199
AHOH1026

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 262
ChainResidue
BHOH1497
BHIS94
BHIS96
BHIS119
BTHR199

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 263
ChainResidue
AHIS94
AHIS119
ALEU198
ATHR199
AHOH1026

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 263
ChainResidue
BHIS94
BHIS119
BLEU198
BTHR199
BHOH1497
BHOH1498

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 264
ChainResidue
ASER48
BLEU182
BLEU185
BPRO186
BPRO187
BTRP189
BHOH1331
BHOH1335
BHOH1573

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues514
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
ATHR199
AHIS64

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
BTHR199
BHIS64

243083

PDB entries from 2025-10-15

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