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2PFG

Crystal structure of human CBR1 in complex with BiGF2.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004090molecular_functioncarbonyl reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006805biological_processxenobiotic metabolic process
A0008106molecular_functionalcohol dehydrogenase (NADP+) activity
A0008211biological_processglucocorticoid metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A0030855biological_processepithelial cell differentiation
A0042373biological_processvitamin K metabolic process
A0046457biological_processprostanoid biosynthetic process
A0047020molecular_function15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity
A0047021molecular_function15-hydroxyprostaglandin dehydrogenase (NADP+) activity
A0050221molecular_functionprostaglandin E2 9-reductase activity
A0070062cellular_componentextracellular exosome
A0160163molecular_functionS-nitrosoglutathione reductase (NADPH) activity
A1903561cellular_componentextracellular vesicle
A2000379biological_processpositive regulation of reactive oxygen species metabolic process
Functional Information from PROSITE/UniProt
site_idPS00061
Number of Residues29
DetailsADH_SHORT Short-chain dehydrogenases/reductases family signature. KgvhqkegwpSsaYGVTKIGVtVLSrIHA
ChainResidueDetails
ALYS180-ALA208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15799708","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17912391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18826943","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P48758","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-1-carboxyethyl lysine","evidences":[{"source":"PubMed","id":"8421682","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
AGLU152
ATYR193
ASER139
ALYS197

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
AASN113
ATYR193
ASER139
ALYS197

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ALYS197
ASER190

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1db3
ChainResidueDetails
ATYR193
ALYS197

238582

PDB entries from 2025-07-09

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