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1FLJ

CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III

Functional Information from GO Data
ChainGOidnamespacecontents
A0004089molecular_functioncarbonate dehydratase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006730biological_processone-carbon metabolic process
A0006979biological_processresponse to oxidative stress
A0008270molecular_functionzinc ion binding
A0009617biological_processresponse to bacterium
A0016151molecular_functionnickel cation binding
A0016791molecular_functionphosphatase activity
A0016829molecular_functionlyase activity
A0045471biological_processresponse to ethanol
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 262
ChainResidue
AHIS94
AHIS96
AHIS119
AHOH312

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GSH A 1183
ChainResidue
ASER182
ACYS183
AARG189
AHOH270
AHOH422
AHOH440
AHOH460
AHOH465
APRO53
AGLU156
AHIS178
APHE179
AASP180

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GSH A 1188
ChainResidue
AGLY171
AALA187
ACYS188
AGLU214

Functional Information from PROSITE/UniProt
site_idPS00162
Number of Residues17
DetailsALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYaaELHLV
ChainResidueDetails
ASER105-VAL121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11024467
ChainResidueDetails
AHIS94
AHIS96
AHIS119

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00918
ChainResidueDetails
ATHR199

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P07450
ChainResidueDetails
AALA2

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER29
ASER43
ASER48
ASER50
ASER55
ASER220

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ATHR73
ATHR130
ATHR217

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ATYR128

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: S-glutathionyl cysteine => ECO:0000269|PubMed:11024467
ChainResidueDetails
ACYS183
ACYS188

218853

PDB entries from 2024-04-24

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