5JAQ
Yersinia pestis FabV variant T276C
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
| A | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue NAI A 401 |
| Chain | Residue |
| A | GLY48 |
| A | GLY110 |
| A | ASP111 |
| A | ALA112 |
| A | SER138 |
| A | LEU139 |
| A | ALA140 |
| A | SER141 |
| A | PHE223 |
| A | THR224 |
| A | TYR225 |
| A | ALA49 |
| A | LEU271 |
| A | LYS272 |
| A | ALA273 |
| A | VAL274 |
| A | CYS276 |
| A | DMS403 |
| A | HOH535 |
| A | HOH541 |
| A | HOH562 |
| A | HOH586 |
| A | SER50 |
| A | HOH625 |
| A | HOH637 |
| A | HOH656 |
| A | THR51 |
| A | GLY52 |
| A | TYR53 |
| A | PHE73 |
| A | PHE74 |
| A | GLU75 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 402 |
| Chain | Residue |
| A | LYS26 |
| A | ASN372 |
| A | GLY377 |
| A | ILE378 |
| A | ASP379 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 403 |
| Chain | Residue |
| A | TYR225 |
| A | TYR235 |
| A | NAI401 |
| A | HOH544 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue DMS A 404 |
| Chain | Residue |
| A | GLU79 |
| A | GLU80 |
| A | LYS106 |
| A | ASP390 |
| A | ASN395 |
| A | ILE397 |
| A | HOH568 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_01838","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22244758","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22244758","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2013","submissionDatabase":"PDB data bank","title":"Enoyl-ACP reductase from Yersinia pestis (wildtype) with cofactor NADH.","authors":["Neckles C.","Hirschbeck M.W.","Shah S.","Pan P.","Bommineni G.R.","Yu W.","Liu N.","Davoodi S.","Kisker C.","Tonge P.J."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01838","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Plays an important role in discriminating NADH against NADPH","evidences":[{"source":"HAMAP-Rule","id":"MF_01838","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
