3ZU2
Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (SIRAS)
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 1423 |
| Chain | Residue |
| A | HIS10 |
| A | GLU98 |
| A | GLY133 |
| A | ASP134 |
| A | ALA135 |
| A | SER161 |
| A | LEU162 |
| A | ALA163 |
| A | SER164 |
| A | PHE246 |
| A | THR247 |
| A | GLY71 |
| A | TYR248 |
| A | LYS267 |
| A | LEU294 |
| A | LYS295 |
| A | ALA296 |
| A | VAL297 |
| A | SER299 |
| A | ALA301 |
| A | SER302 |
| A | NA1424 |
| A | ALA72 |
| A | HOH2057 |
| A | HOH2096 |
| A | HOH2097 |
| A | HOH2121 |
| A | SER73 |
| A | THR74 |
| A | GLY75 |
| A | TYR76 |
| A | PHE96 |
| A | PHE97 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1424 |
| Chain | Residue |
| A | GLY71 |
| A | THR74 |
| A | TYR76 |
| A | GLY77 |
| A | SER161 |
| A | NAI1423 |
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 |
