3Q6I
Crystal structure of FabG4 and coenzyme binary complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid 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 | 0047025 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid 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 | 0047025 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) activity |
| C | 0006629 | biological_process | lipid metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0047025 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) activity |
| D | 0006629 | biological_process | lipid metabolic process |
| D | 0006631 | biological_process | fatty acid metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0047025 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADH) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD A 1 |
| Chain | Residue |
| A | GLY220 |
| A | GLY297 |
| A | VAL318 |
| A | LEU345 |
| A | SER346 |
| A | TYR360 |
| A | LYS364 |
| A | PRO390 |
| A | ILE393 |
| A | THR395 |
| A | MET397 |
| A | ARG223 |
| A | THR398 |
| A | HOH459 |
| A | HOH500 |
| A | HOH519 |
| A | HOH523 |
| A | ILE225 |
| A | ASP244 |
| A | LEU266 |
| A | ASP267 |
| A | VAL268 |
| A | ASN295 |
| A | ALA296 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZPG A 455 |
| Chain | Residue |
| A | ASN354 |
| A | HOH520 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD B 3 |
| Chain | Residue |
| B | GLY220 |
| B | ARG223 |
| B | ILE225 |
| B | ASP244 |
| B | VAL245 |
| B | LEU266 |
| B | ASP267 |
| B | VAL268 |
| B | ASN295 |
| B | GLY297 |
| B | LEU345 |
| B | TYR360 |
| B | LYS364 |
| B | GLY391 |
| B | ILE393 |
| B | THR395 |
| B | THR398 |
| B | HOH488 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAD C 2 |
| Chain | Residue |
| C | HOH7 |
| C | GLY220 |
| C | ARG223 |
| C | GLY224 |
| C | ILE225 |
| C | ASP244 |
| C | LEU266 |
| C | ASP267 |
| C | VAL268 |
| C | ASN295 |
| C | ILE298 |
| C | SER347 |
| C | TYR360 |
| C | LYS364 |
| C | PRO390 |
| C | GLY391 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD D 4 |
| Chain | Residue |
| D | GLY220 |
| D | ARG223 |
| D | ILE225 |
| D | ASP244 |
| D | VAL245 |
| D | LEU266 |
| D | ASP267 |
| D | VAL268 |
| D | ASN295 |
| D | ALA296 |
| D | GLY297 |
| D | VAL318 |
| D | LEU345 |
| D | SER347 |
| D | TYR360 |
| D | LYS364 |
| D | GLY391 |
| D | ILE393 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SiagiagnrgQtnYATTKAGMiGITqALA |
| Chain | Residue | Details |
| A | SER347-ALA375 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23163771","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V1U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FW8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23163771","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of holoFabG4.","authors":["Dutta D.","Bhattacharyya S.","Das A.K."]}},{"source":"PDB","id":"3Q6I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3V1U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FW8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23163771","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
