Research workbench
X-ray structure of enoyl-acyl carrier protein reductase from bacillus anthracis with NAD+
Analyse X-ray structure of enoyl-acyl carrier protein reductase from bacillus anthracis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YCR
- Type
- protein
- Length
- 999 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q81GI3
- Ligands
- NAD, SO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 250 | — | Q81GI3 |
| C | — | protein | 250 | — | Q81GI3 |
| D | — | protein | 249 | — | Q81GI3 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 15 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YCR · X-Ray Structure of Enoyl-Acyl Carrier Protein Reductase from Bacillus Anthracis with NAD+ · the same entry in another collection · chain D against D, TM-score 1.00
- Q81GI3 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH] fabi… · a predicted model of the same protein · chain C against A, TM-score 0.99
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 Q81GI3
- Elsewhere: RCSB PDB 5YCR · PDBe 5YCR · UniProt Q81GI3
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