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4QJP

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
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
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 B 301
ChainResidue
BHIS96
BHIS98
BHIS121
BV1F303

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PEG B 302
ChainResidue
BLEU253
BLYS254
BARG256
ALYS59
AILE60
AARG177
BASP28
BGLN29

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE V1F B 303
ChainResidue
BSER64
BHIS66
BASN69
BGLN94
BHIS96
BHIS98
BHIS121
BVAL123
BPHE133
BALA137
BLEU200
BTHR201
BVAL202
BPRO204
BZN301
BHOH608
BHOH637
BHOH639

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 304
ChainResidue
BGLY100
BSER101
BHIS105
BSER245
BHIS247
BHOH420

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
AHIS96
AHIS98
AHIS121
AV1F303

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CIT A 302
ChainResidue
AGLY100
ASER101
AHIS105
ASER245
AHIS247
AHOH485
AHOH618
BHOH499

site_idAC7
Number of Residues18
DetailsBINDING SITE FOR RESIDUE V1F A 303
ChainResidue
AHIS66
AASN69
AGLN94
AHIS96
AHIS98
AHIS121
AVAL123
APHE133
AVAL145
ALEU200
ATHR201
AVAL202
ATRP211
AZN301
AHOH487
AHOH590
AHOH641
AHOH643

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AGLN160
AGLN223
ALYS227
AHOH458
AHOH611
AHOH614

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
ALEU166
AASP167
ALYS170
ASER230

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 306
ChainResidue
AASP104
AVAL114
ASER115
ASER157
AHOH639

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHiVdgvsYaaELHVV
ChainResidueDetails
BSER107-VAL123

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
BHIS66
AHIS66

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:18618712
ChainResidueDetails
BHIS96
BHIS98
BHIS121
AHIS96
AHIS98
AHIS121

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
BTHR201
ATHR201

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PDB entries from 2024-07-24

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