1NFF
Crystal structure of Rv2002 gene product from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006706 | biological_process | steroid catabolic process |
| A | 0008202 | biological_process | steroid 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 | 0047023 | molecular_function | androsterone dehydrogenase [NAD(P)+] activity |
| A | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase (NAD+) activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006706 | biological_process | steroid catabolic process |
| B | 0008202 | biological_process | steroid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0047023 | molecular_function | androsterone dehydrogenase [NAD(P)+] activity |
| B | 0047044 | molecular_function | androstan-3-alpha,17-beta-diol dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD A 1300 |
| Chain | Residue |
| A | GLY14 |
| A | VAL62 |
| A | ASN88 |
| A | ALA89 |
| A | GLY90 |
| A | ILE91 |
| A | ILE138 |
| A | SER139 |
| A | SER140 |
| A | TYR153 |
| A | LYS157 |
| A | ARG17 |
| A | PRO183 |
| A | GLY184 |
| A | VAL186 |
| A | THR188 |
| A | PRO189 |
| A | MET190 |
| A | THR191 |
| A | HOH1302 |
| A | HOH1315 |
| A | HOH1318 |
| A | GLY18 |
| A | HOH1326 |
| A | HOH1376 |
| A | HOH1449 |
| A | MET19 |
| A | ASP38 |
| A | ILE39 |
| A | LEU40 |
| A | LEU60 |
| A | ASP61 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 2300 |
| Chain | Residue |
| B | GLY14 |
| B | ARG17 |
| B | GLY18 |
| B | MET19 |
| B | ASP38 |
| B | LEU40 |
| B | LEU60 |
| B | ASP61 |
| B | VAL62 |
| B | ASN88 |
| B | GLY90 |
| B | ILE91 |
| B | ILE138 |
| B | SER139 |
| B | SER140 |
| B | TYR153 |
| B | LYS157 |
| B | PRO183 |
| B | GLY184 |
| B | VAL186 |
| B | THR188 |
| B | PRO189 |
| B | MET190 |
| B | THR191 |
| B | HOH2302 |
| B | HOH2312 |
| B | HOH2351 |
| B | HOH2353 |
| B | HOH2402 |
| B | HOH2463 |
| B | HOH2477 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SieglagtvaChgYTATKFAVrGLTkSTA |
| Chain | Residue | Details |
| A | SER140-ALA168 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12524453","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12524453","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NFF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NFQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NFR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12524453","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NFF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NFR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12524453","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NFF","evidenceCode":"ECO:0007744"}]} |
| 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 | GLU142 | |
| A | SER140 | |
| A | LYS157 | |
| A | TYR153 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | LYS157 | |
| B | TYR153 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | GLU142 | |
| B | SER140 | |
| B | LYS157 | |
| B | TYR153 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | SER140 | |
| A | LYS157 | |
| A | TYR153 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | SER140 | |
| B | LYS157 | |
| B | TYR153 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | SER140 | |
| A | ASN112 | |
| A | LYS157 | |
| A | TYR153 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | SER140 | |
| B | ASN112 | |
| B | LYS157 | |
| B | TYR153 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | CYS150 | |
| A | LYS157 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| B | CYS150 | |
| B | LYS157 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1db3 |
| Chain | Residue | Details |
| A | LYS157 | |
| A | TYR153 |
