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1FLJ

CRYSTAL STRUCTURE OF S-GLUTATHIOLATED CARBONIC ANHYDRASE III

Functional Information from GO Data
ChainGOidnamespacecontents
A0003009biological_processskeletal muscle contraction
A0004089molecular_functioncarbonate dehydratase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0008270molecular_functionzinc ion binding
A0008284biological_processpositive regulation of cell population proliferation
A0016791molecular_functionphosphatase activity
A0016829molecular_functionlyase activity
A0030017cellular_componentsarcomere
A0032869biological_processcellular response to insulin stimulus
A0033993biological_processresponse to lipid
A0043066biological_processnegative regulation of apoptotic process
A0044320biological_processcellular response to leptin stimulus
A0045471biological_processresponse to ethanol
A0046872molecular_functionmetal ion binding
A0071456biological_processcellular response to hypoxia
A0097305biological_processresponse to alcohol
A0097421biological_processliver regeneration
A1903427biological_processnegative regulation of reactive oxygen species biosynthetic process
A1903751biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide
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
DetailsRegion: {"description":"Involved in proton transfer","evidences":[{"source":"UniProtKB","id":"P07451","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11024467","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P07450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"S-glutathionyl cysteine","evidences":[{"source":"PubMed","id":"11024467","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ca2
ChainResidueDetails
ATHR199
ALYS64

248942

PDB entries from 2026-02-11

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