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Crystal structure of the flagellar cap protein flid D2-D3 domains from serratia marcescens in space group I422
Analyse Crystal structure of the flagellar cap protein flid D2-D3 domains from serratia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XLK
- Type
- protein
- Length
- 563 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flagellar hook-associated protein 2
- UniProt
- A0A0P0QFX8
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Flagellar hook-associated protein 2 | protein | 189 | 11% helix, 43% strand | A0A0P0QFX8 |
| C | Flagellar hook-associated protein 2 | protein | 185 | 11% helix, 45% strand | A0A0P0QFX8 |
Ligands and binding sites
- ZN · Zinc ion · metal · 9 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.44 | 0.82 | 14 | empty |
| 2 | 59 | 0.43 | 0.82 | 19 | empty |
| 3 | 104 | 0.38 | 0.75 | 18 | empty |
| 4 | 91 | 0.36 | 0.75 | 18 | empty |
| 5 | 59 | 0.33 | 0.77 | 20 | ZN |
Interfaces
2 interfaces between chains.
- A–B · 824 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 420 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5XLK · Crystal structure of the flagellar cap protein FliD D2-D3 domains from Serratia… · 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 A0A0P0QFX8
- Elsewhere: RCSB PDB 5XLK · PDBe 5XLK · UniProt A0A0P0QFX8
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