5G2O
Yersinia pestis FabV variant T276A
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 | 33 |
| Details | BINDING SITE FOR RESIDUE NAI A 1400 |
| 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 | GLN277 |
| A | DMS1402 |
| A | HOH2150 |
| A | HOH2156 |
| A | HOH2216 |
| A | HOH2220 |
| A | SER50 |
| A | HOH2221 |
| A | HOH2222 |
| A | HOH2323 |
| A | HOH2324 |
| 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 1401 |
| Chain | Residue |
| A | ASN372 |
| A | GLY377 |
| A | ILE378 |
| A | ASP379 |
| A | HOH2325 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 1402 |
| Chain | Residue |
| A | TYR225 |
| A | TYR235 |
| A | NAI1400 |
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 |
