Research workbench
Structure of the 328-692 fragment of flha (orthorhombic form)
Analyse Structure of the 328-692 fragment of flha (orthorhombic form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AI0
- Type
- protein
- Length
- 668 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar biosynthesis protein flha
- UniProt
- P40729
- Ligands
- CA
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar biosynthesis protein flha | protein | 333 | 46% helix, 17% strand | P40729 |
| B | Flagellar biosynthesis protein flha | protein | 335 | 45% helix, 17% strand | P40729 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A, B
- MRD · (4R)-2-methylpentane-2,4-diol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1140 | 0.74 | 0.77 | 73 | empty |
| 2 | 130 | 0.45 | 0.77 | 15 | MRD |
| 3 | 112 | 0.44 | 0.78 | 20 | MRD |
| 4 | 78 | 0.40 | 0.79 | 19 | empty |
| 5 | 101 | 0.35 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 657 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6AI0 · Structure of the 328-692 fragment of FlhA (orthorhombic form) · the same entry in another collection · chain A against A, TM-score 1.00
- P40729 · AlphaFold monomer V2.0 prediction for flagellar biosynthesis protein flha (P40729) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P40729
- Elsewhere: RCSB PDB 6AI0 · PDBe 6AI0 · UniProt P40729
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