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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
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
A0019371biological_processcyclooxygenase pathway
A0030855biological_processepithelial cell differentiation
A0042373biological_processvitamin K metabolic process
A0047020molecular_function15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity
A0047021molecular_function15-hydroxyprostaglandin dehydrogenase (NADP+) activity
A0050221molecular_functionprostaglandin-E2 9-reductase activity
A0070062cellular_componentextracellular exosome
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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR193

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:15799708, ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943
ChainResidueDetails
AVAL9
AASP62
AASN89
ATYR193
AVAL230

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
APHE94
AGLN105
ASER139
AALA192

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47727
ChainResidueDetails
ASER1

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48758
ChainResidueDetails
ASER29

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-1-carboxyethyl lysine => ECO:0000269|PubMed:8421682
ChainResidueDetails
ALYS238

218853

PDB entries from 2024-04-24

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