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5E2M

Crystal structure of human carbonic anhydrase isozyme I with 3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide

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
AV14302

site_idAC2
Number of Residues19
Detailsbinding site for residue V14 A 302
ChainResidue
AHIS119
ALEU131
AALA135
ALEU198
ATHR199
AHIS200
APRO201
APRO202
ATRP209
AZN301
AACT303
AHOH489
AHOH518
BALA132
AHIS64
AHIS67
APHE91
AHIS94
AHIS96

site_idAC3
Number of Residues4
Detailsbinding site for residue ACT A 303
ChainResidue
ATYR204
AV14302
AHOH402
BTYR204

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
BV14302

site_idAC5
Number of Residues14
Detailsbinding site for residue V14 B 302
ChainResidue
BHIS64
BHIS67
BGLN92
BHIS94
BHIS96
BHIS119
BALA135
BLEU198
BTHR199
BHIS200
BPRO201
BPRO202
BZN301
BHOH591

site_idAC6
Number of Residues7
Detailsbinding site for residue PEG B 303
ChainResidue
ALYS172
AHOH413
AHOH415
BASN52
BPRO53
BALA54
BASN178

site_idAC7
Number of Residues8
Detailsbinding site for residue PEG B 304
ChainResidue
BASP74
BASN75
BARG76
BALA153
BPRO155
BGLN158
BHOH506
BHOH602

site_idAC8
Number of Residues15
Detailsbinding site for Di-peptide ASP B 72 and ARG B 89
ChainResidue
BPHE70
BGLU71
BASN73
BASP74
BASN75
BSER77
BTYR88
BLEU90
BPHE91
BHIS122
BTRP123
BHOH401
BHOH430
BHOH567
BHOH569

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

224201

PDB entries from 2024-08-28

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