1WMA
Crystal structure of human CBR1 in complex with Hydroxy-PP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006805 | biological_process | xenobiotic metabolic process |
A | 0008106 | molecular_function | alcohol dehydrogenase (NADP+) activity |
A | 0008211 | biological_process | glucocorticoid metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
A | 0019371 | biological_process | cyclooxygenase pathway |
A | 0030855 | biological_process | epithelial cell differentiation |
A | 0042373 | biological_process | vitamin K metabolic process |
A | 0047020 | molecular_function | 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity |
A | 0047021 | molecular_function | 15-hydroxyprostaglandin dehydrogenase (NADP+) activity |
A | 0050221 | molecular_function | prostaglandin E2 9-reductase activity |
A | 0070062 | cellular_component | extracellular exosome |
A | 0160163 | molecular_function | S-nitrosoglutathione reductase (NADPH) activity |
A | 1903561 | cellular_component | extracellular vesicle |
A | 2000379 | biological_process | positive regulation of reactive oxygen species metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 300 |
Chain | Residue |
A | ARG57 |
A | PHE58 |
A | HOH542 |
A | HOH639 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 301 |
Chain | Residue |
A | SO4305 |
A | HOH424 |
A | HOH458 |
A | HOH553 |
A | HOH559 |
A | PHE102 |
A | SER190 |
A | SER191 |
A | ALA192 |
A | TYR193 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | LYS216 |
A | GLY217 |
A | ASP218 |
A | LYS219 |
A | HOH506 |
A | HOH511 |
A | HOH761 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 303 |
Chain | Residue |
A | ASP64 |
A | LYS111 |
A | THR163 |
A | ARG209 |
A | LYS210 |
A | GLU213 |
A | HOH446 |
A | HOH460 |
A | HOH677 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 304 |
Chain | Residue |
A | ARG41 |
A | ARG118 |
A | HOH571 |
A | HOH656 |
A | HOH675 |
A | HOH684 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 305 |
Chain | Residue |
A | VAL96 |
A | ALA97 |
A | ARG272 |
A | SO4301 |
A | HOH502 |
A | HOH553 |
A | HOH559 |
A | HOH576 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 306 |
Chain | Residue |
A | SER2 |
A | GLY3 |
A | GLN47 |
A | GLN50 |
A | LYS129 |
A | HOH742 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE AB3 A 307 |
Chain | Residue |
A | SER139 |
A | MET141 |
A | TYR193 |
A | GLY228 |
A | TRP229 |
A | AB3308 |
A | NDP309 |
A | PE5310 |
A | HOH479 |
site_id | AC9 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE AB3 A 308 |
Chain | Residue |
A | ARG22 |
A | ARG26 |
A | ILE140 |
A | ARG144 |
A | GLU244 |
A | AB3307 |
A | PE5310 |
A | HOH484 |
A | HOH607 |
A | HOH642 |
site_id | BC1 |
Number of Residues | 39 |
Details | BINDING SITE FOR RESIDUE NDP A 309 |
Chain | Residue |
A | HOH430 |
A | HOH449 |
A | HOH481 |
A | HOH523 |
A | HOH549 |
A | HOH661 |
A | HOH664 |
A | HOH666 |
A | HOH721 |
A | GLY11 |
A | ASN13 |
A | LYS14 |
A | GLY15 |
A | ILE16 |
A | ARG37 |
A | LEU61 |
A | ASP62 |
A | ILE63 |
A | ASP64 |
A | ASN89 |
A | ALA90 |
A | GLY91 |
A | ILE92 |
A | VAL137 |
A | SER138 |
A | TYR193 |
A | LYS197 |
A | PRO227 |
A | GLY228 |
A | TRP229 |
A | VAL230 |
A | THR232 |
A | ASP233 |
A | MET234 |
A | ALA235 |
A | AB3307 |
A | HOH402 |
A | HOH406 |
A | HOH407 |
site_id | BC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PE5 A 310 |
Chain | Residue |
A | ASP23 |
A | ALA93 |
A | MET141 |
A | ARG144 |
A | MET234 |
A | GLU248 |
A | TYR252 |
A | AB3307 |
A | AB3308 |
A | HOH416 |
A | HOH423 |
A | HOH466 |
A | HOH495 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE P33 A 311 |
Chain | Residue |
A | ALA93 |
A | THR122 |
A | LEU125 |
A | HIS207 |
A | LYS210 |
A | LEU211 |
A | GLN214 |
A | HOH623 |
A | HOH697 |
A | HOH730 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. KgvhqkegwpSsaYGVTKIGVtVLSrIHA |
Chain | Residue | Details |
A | LYS180-ALA208 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | GLY194 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15799708, ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943 |
Chain | Residue | Details |
A | THR10 | |
A | ILE63 | |
A | ALA90 | |
A | GLY194 | |
A | ARG231 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS95 | |
A | ALA106 | |
A | ILE140 | |
A | TYR193 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47727 |
Chain | Residue | Details |
A | SER2 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48758 |
Chain | Residue | Details |
A | GLY30 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-1-carboxyethyl lysine => ECO:0000269|PubMed:8421682 |
Chain | Residue | Details |
A | ALA239 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | GLU152 | |
A | TYR193 | |
A | SER139 | |
A | LYS197 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | ASN113 | |
A | TYR193 | |
A | SER139 | |
A | LYS197 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | LYS197 | |
A | SER190 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1db3 |
Chain | Residue | Details |
A | TYR193 | |
A | LYS197 |