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 | 0018455 | molecular_function | alcohol dehydrogenase [NAD(P)+] activity |
| A | 0030855 | biological_process | epithelial cell differentiation |
| A | 0042373 | biological_process | vitamin K metabolic process |
| A | 0046457 | biological_process | prostanoid biosynthetic 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 | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15799708","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17912391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18826943","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P48758","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-1-carboxyethyl lysine","evidences":[{"source":"PubMed","id":"8421682","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 |
