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5GMM

Crystal structure of human Carbonic anhydrase I in complex with polmacoxib

Functional Information from GO Data
ChainGOidnamespacecontents
A0004064molecular_functionarylesterase activity
A0004089molecular_functioncarbonate dehydratase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0018820molecular_functioncyanamide hydratase activity
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
B0004064molecular_functionarylesterase activity
B0004089molecular_functioncarbonate dehydratase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0016829molecular_functionlyase activity
B0016836molecular_functionhydro-lyase activity
B0018820molecular_functioncyanamide hydratase activity
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
A949302

site_idAC2
Number of Residues14
Detailsbinding site for residue 949 A 302
ChainResidue
ALEU131
AALA135
ALEU198
ATHR199
AHIS200
ATRP209
AZN301
A949303
A949304
AHIS64
AHIS67
AHIS94
AHIS96
AHIS119

site_idAC3
Number of Residues12
Detailsbinding site for residue 949 A 303
ChainResidue
AILE60
AASN61
AVAL62
AHIS67
AASN69
APHE91
AGLN92
ALYS170
A949302
A949304
BALA132
B949305

site_idAC4
Number of Residues9
Detailsbinding site for residue 949 A 304
ChainResidue
AALA132
ASER136
ATYR204
A949302
A949303
AHOH482
BLYS170
B949304
B949305

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
B949303

site_idAC6
Number of Residues15
Detailsbinding site for residue 949 B 303
ChainResidue
BHIS64
BHIS67
BHIS94
BHIS96
BHIS119
BLEU131
BALA135
BVAL143
BLEU198
BTHR199
BHIS200
BTRP209
BZN301
B949304
B949305

site_idAC7
Number of Residues10
Detailsbinding site for residue 949 B 304
ChainResidue
AALA132
A949304
BASN61
BVAL62
BHIS67
BASN69
BGLN92
BLYS170
B949303
B949305

site_idAC8
Number of Residues11
Detailsbinding site for residue 949 B 305
ChainResidue
A949303
A949304
BTRP5
BTYR20
BALA132
BALA135
BPRO201
BPRO202
B949303
B949304
BHOH517

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYsaELHVA
ChainResidueDetails
ASER105-ALA121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
AHIS64
BHIS64

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: in variant Michigan-1 => ECO:0000269|PubMed:12009884
ChainResidueDetails
AHIS64
AHIS67
AHIS200
BHIS64
BHIS67
BHIS200

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362
ChainResidueDetails
AHIS94
AHIS96
AHIS119
BHIS94
BHIS96
BHIS119

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8057362
ChainResidueDetails
ATHR199
BTHR199

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:4207120, ECO:0000269|PubMed:4217196
ChainResidueDetails
AALA1
BALA1

224572

PDB entries from 2024-09-04

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