Research workbench
NADH bound structure of fabmg, novel type of enoyl-acyl carrier protein reductase
Analyse NADH bound structure of fabmg, novel type of enoyl-acyl carrier protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KIA
- Type
- protein
- Length
- 1,249 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1C9HA64
- Ligands
- NAI
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 442 | — | A0A1C9HA64 |
| B | — | protein | 440 | — | A0A1C9HA64 |
| C | — | protein | 367 | — | A0A1C9HA64 |
Ligands and binding sites
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6KIA · NADH bound structure of FabMG, novel type of Enoyl-acyl carrier protein reductase · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A1C9HA64
- Elsewhere: RCSB PDB 6KIA · PDBe 6KIA · UniProt A0A1C9HA64
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