Research workbench
Structure of Mycobacterium tuberculosis Fatty Acid Synthase - I
Analyse Structure of Mycobacterium tuberculosis Fatty Acid Synthase - I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GJC
- Type
- protein
- Length
- 16,620 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.3
- Source
- Mycobacterium tuberculosis
- Molecule
- Fatty acid synthase
- EC
- 2.3.1.41
- UniProt
- A0A0T9Z6H1
- Ligands
- FMN
- Pockets
- 20 · best druggability 0.89
Structure
electron microscopy · resolution 3.3 · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Fatty acid synthase (EC 2.3.1.41) | protein | 2770 | 41% helix, 16% strand | A0A0T9Z6H1 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 975 | 0.89 | 0.91 | 104 | empty |
| 2 | 1128 | 0.88 | 0.89 | 127 | empty |
| 3 | 374 | 0.87 | 0.95 | 60 | empty |
| 4 | 1109 | 0.84 | 0.85 | 127 | empty |
| 5 | 1072 | 0.84 | 0.85 | 131 | empty |
Interfaces
15 interfaces between chains.
- C–D · 3697 Ų buried · 34 hydrogen bonds · protein-protein
- B–E · 3691 Ų buried · 33 hydrogen bonds · protein-protein
- A–F · 3676 Ų buried · 30 hydrogen bonds · protein-protein
- A–E · 2165 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 2046 Ų buried · 14 hydrogen bonds · protein-protein
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 A0A0T9Z6H1
- Elsewhere: RCSB PDB 6GJC · PDBe 6GJC · UniProt A0A0T9Z6H1
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