MolNFT v1 · #164696 · protein
Crsytal structure of acinetobacter baumannii fabg inhibitor complex at 2.35 a resolution
6T65: “Crsytal structure of acinetobacter baumannii fabg inhibitor complex at 2.35 a resolution”. X-ray diffraction, 1 ligand (MLH). MolNFT v1 #164696 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6T65
- Type
- protein
- Length
- 904 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- V5VHN7
- Ligands
- MLH
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 242 | — | V5VHN7 |
| B | — | protein | 231 | — | V5VHN7 |
| C | — | protein | 218 | — | V5VHN7 |
| D | — | protein | 213 | — | 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.
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
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