2HRB
Crystal Structure of human Carbonyl Reductase 3, complexed with NADP+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000253 | molecular_function | 3-beta-hydroxysteroid 3-dehydrogenase (NADP+) activity |
| A | 0004090 | molecular_function | carbonyl reductase (NADPH) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0008753 | molecular_function | NADPH dehydrogenase (quinone) activity |
| 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 | 0042376 | biological_process | phylloquinone catabolic process |
| A | 0050890 | biological_process | cognition |
| A | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP A 1001 |
| Chain | Residue |
| A | GLY12 |
| A | ILE64 |
| A | ASP65 |
| A | ASN90 |
| A | ALA91 |
| A | ALA92 |
| A | ILE138 |
| A | SER139 |
| A | TYR194 |
| A | LYS198 |
| A | PRO228 |
| A | ASN14 |
| A | GLY229 |
| A | VAL231 |
| A | ASP239 |
| A | GOL2001 |
| A | HOH2006 |
| A | HOH2012 |
| A | HOH2017 |
| A | HOH2036 |
| A | HOH2060 |
| A | HOH2076 |
| A | ARG15 |
| A | HOH2139 |
| A | HOH2169 |
| A | GLY16 |
| A | ILE17 |
| A | ARG38 |
| A | ARG42 |
| A | LEU62 |
| A | ASP63 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 2001 |
| Chain | Residue |
| A | ALA92 |
| A | VAL93 |
| A | ALA94 |
| A | TYR194 |
| A | NAP1001 |
| A | HOH2169 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 2002 |
| Chain | Residue |
| A | HIS159 |
| A | ARG206 |
| A | ASN276 |
| A | TRP277 |
| A | HOH2130 |
| A | HOH2135 |
| A | HOH2219 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 2003 |
| Chain | Residue |
| A | ARG38 |
| A | ASP39 |
| A | VAL40 |
| A | ALA41 |
| A | ARG78 |
| A | GLY82 |
| A | PRO127 |
| A | ILE128 |
| A | HOH2030 |
| A | HOH2108 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. NevheregwpNspYGVSKLGVtVLSrILA |
| Chain | Residue | Details |
| A | ASN181-ALA209 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 35 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human carbonyl reductase 3, complexed with NADP+.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | GLN142 | |
| A | SER140 | |
| A | LYS198 | |
| A | TYR194 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS198 | |
| A | SER140 | |
| A | TYR194 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | ASN114 | |
| A | LYS198 | |
| A | SER140 | |
| A | TYR194 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS198 | |
| A | ASN191 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS198 | |
| A | TYR194 |
