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4QJX

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
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0043209cellular_componentmyelin sheath
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS96
AHIS98
AHIS121
AWWO304

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG A 302
ChainResidue
ASER190
AGLN216
AHOH503
AHOH598

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
AARG177
APHE178
ATHR179
AHOH593
ALYS161

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE WWO A 304
ChainResidue
ASER64
AHIS66
AASN69
AHIS96
AHIS98
AHIS121
APHE133
AALA137
ALEU200
ATHR201
AVAL202
AZN301
AHOH546

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 Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS66

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:18618712
ChainResidueDetails
AHIS96
AHIS98
AHIS121

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR201

222036

PDB entries from 2024-07-03

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