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6SWM

selenol bound 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 Residues5
Detailsbinding site for residue ZN A 301
ChainResidue
AHIS94
AHIS96
AHIS119
ATHR199
ALVW302

site_idAC2
Number of Residues7
Detailsbinding site for residue LVW A 302
ChainResidue
ATHR199
ATRP209
AZN301
AGLN92
AHIS94
AHIS119
AVAL143

site_idAC3
Number of Residues5
Detailsbinding site for residue ZN B 301
ChainResidue
BHIS94
BHIS96
BHIS119
BTHR199
BLVW302

site_idAC4
Number of Residues9
Detailsbinding site for residue LVW B 302
ChainResidue
BGLN92
BHIS94
BHIS119
BVAL143
BLEU198
BTHR199
BTRP209
BZN301
BHOH432

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

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PDB entries from 2024-11-06

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