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2NN7

Structure of inhibitor binding to Carbonic Anhydrase I

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
AM29311

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 302
ChainResidue
BHIS94
BHIS96
BHIS119
BM29312

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE M29 A 311
ChainResidue
AGLN92
AHIS94
AHIS96
AHIS119
AVAL143
ALEU198
ATHR199
AHIS200
ATRP209
AZN301
BALA132
AASN69

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE M29 B 312
ChainResidue
AHOH549
BASN69
BPHE91
BGLN92
BHIS94
BHIS96
BHIS119
BLEU198
BTHR199
BHIS200
BTRP209
BZN302

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DMS A 341
ChainResidue
ATHR35
ATHR38
ATRP192
APHE260

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
ASER65
BSER65

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: in variant Michigan-1 => ECO:0000269|PubMed:12009884
ChainResidueDetails
ASER65
AVAL68
APRO201
BSER65
BVAL68
BPRO201

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
APHE95
ATRP97
AVAL120
BPHE95
BTRP97
BVAL120

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8057362
ChainResidueDetails
AHIS200
BHIS200

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:4207120, ECO:0000269|PubMed:4217196
ChainResidueDetails
ASER2
BSER2

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR199
AHIS64

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
BTHR199
BHIS64

222926

PDB entries from 2024-07-24

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