3BHM
Crystal structure of human Carbonyl Reductase 1 in complex with S-hydroxymethylglutathione
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 | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | ARG57 |
| A | PHE58 |
| A | HOH522 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | LYS14 |
| A | GLY15 |
| A | HOH408 |
| A | HOH432 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | HOH599 |
| A | ARG118 |
| A | HOH539 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | LYS216 |
| A | GLY217 |
| A | ASP218 |
| A | LYS219 |
| A | HOH479 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE AHE A 304 |
| Chain | Residue |
| A | ALA93 |
| A | PHE94 |
| A | LYS95 |
| A | PHE102 |
| A | GLN105 |
| A | SER190 |
| A | SER191 |
| A | ALA192 |
| A | TYR193 |
| A | MET234 |
| A | HOH416 |
| A | HOH459 |
| A | HOH521 |
| A | HOH603 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE AB3 A 307 |
| Chain | Residue |
| A | LEU27 |
| A | SER139 |
| A | TYR193 |
| A | GLY228 |
| A | TRP229 |
| A | HOH561 |
| A | HOH603 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE AB3 A 308 |
| Chain | Residue |
| A | ARG22 |
| A | ARG26 |
| A | ILE140 |
| A | ARG144 |
| A | GLU244 |
| site_id | AC8 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAP A 309 |
| Chain | Residue |
| 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 | SER138 |
| A | TYR193 |
| A | LYS197 |
| A | PRO227 |
| A | GLY228 |
| A | TRP229 |
| A | THR232 |
| A | ASP233 |
| A | MET234 |
| A | ALA235 |
| A | HOH406 |
| A | HOH410 |
| A | HOH413 |
| A | HOH431 |
| A | HOH432 |
| A | HOH470 |
| A | HOH477 |
| A | HOH481 |
| A | HOH512 |
| A | HOH590 |
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 |
