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4QIZ

Crystal structure of human carbonic anhydrase isozyme XIII 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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS96
AHIS98
AHIS121
AWWX304

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
ALYS161
AARG177
APHE178
ATHR179
AHOH436

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AASP112
AGLY113
AGLN160
AGLN223
AGLN224
AHOH478
AHOH491
AHOH592

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE WWX A 304
ChainResidue
ASER64
AASN69
AGLN94
AHIS96
AHIS98
AHIS121
APHE133
ALEU200
ATHR201
AVAL202
APRO204
AZN301
AHOH553
AHOH589

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BHIS96
BHIS98
BHIS121
BWWX303

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 302
ChainResidue
BSER222
BALA226
BHOH566

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE WWX B 303
ChainResidue
BSER64
BASN69
BGLN94
BHIS96
BHIS98
BHIS121
BVAL123
BALA137
BLEU200
BTHR201
BVAL202
BZN301
BHOH447
BHOH584
BHOH616

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHiVdgvsYaaELHVV
ChainResidueDetails
ASER107-VAL123

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":"18618712","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

239149

PDB entries from 2025-07-23

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