Research workbench
Crystal structure of fabg from bacillus sp
Analyse Crystal structure of fabg from bacillus sp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NBU
- Type
- protein
- Length
- 970 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-(acyl-carrier-protein) reductase
- UniProt
- A6CQL2
- Ligands
- NAI, CAA
- Pockets
- 8 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | 3-oxoacyl-(acyl-carrier-protein) reductase | protein | 242 | 52% helix, 17% strand | A6CQL2 |
| B | 3-oxoacyl-(acyl-carrier-protein) reductase | protein | 244 | 52% helix, 17% strand | A6CQL2 |
Ligands and binding sites
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- CAA · Acetoacetyl-coenzyme A · ligand · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1034 | 0.87 | 0.88 | 81 | empty |
| 2 | 562 | 0.74 | 0.81 | 55 | NAI |
| 3 | 577 | 0.73 | 0.81 | 62 | NAI, CAA |
| 4 | 544 | 0.71 | 0.80 | 63 | NAI |
| 5 | 399 | 0.69 | 0.81 | 47 | NAI |
Interfaces
6 interfaces between chains.
- B–D · 1588 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 1553 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 1364 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1358 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 154 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4NBU · Crystal structure of FabG from Bacillus sp · 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 A6CQL2
- Elsewhere: RCSB PDB 4NBU · PDBe 4NBU · UniProt A6CQL2
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