Research workbench
Crsytal structure of acinetobacter baumannii fabg inhibitor complex at 2.35 a resolution
Analyse Crsytal structure of acinetobacter baumannii fabg inhibitor complex at 2.35 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T65
- Type
- protein
- Length
- 904 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-oxoacyl-(acyl-carrier-protein) reductase
- EC
- 1.1.1.100
- UniProt
- V5VHN7
- Ligands
- MLH
- Pockets
- 11 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-oxoacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100) | protein | 242 | 51% helix, 18% strand | V5VHN7 |
| B | 3-oxoacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100) | protein | 231 | 52% helix, 18% strand | V5VHN7 |
| C | 3-oxoacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100) | protein | 218 | 48% helix, 19% strand | V5VHN7 |
| D | 3-oxoacyl-(acyl-carrier-protein) reductase (EC 1.1.1.100) | protein | 213 | 47% helix, 19% strand | V5VHN7 |
Ligands and binding sites
- MLH · ethyl 6-bromanyl-2-[(dimethylamino)methyl]-5-oxidanyl-1-phenyl-indole-3-carboxylate · ligand · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1157 | 0.83 | 0.84 | 91 | empty |
| 2 | 292 | 0.79 | 0.90 | 32 | MLH |
| 3 | 412 | 0.72 | 0.83 | 41 | empty |
| 4 | 388 | 0.61 | 0.77 | 39 | empty |
| 5 | 50 | 0.61 | 0.93 | 15 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1644 Ų buried · 27 hydrogen bonds · protein-protein
- A–D · 1563 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1559 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1200 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 152 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6T65 · Crsytal structure of Acinetobacter baumannii FabG inhibitor complex at 2.35 A resolution · 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 V5VHN7
- Elsewhere: RCSB PDB 6T65 · PDBe 6T65 · UniProt V5VHN7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.