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Crystal structure of truncated flgd (monoclinic form) from the human pathogen helicobacter pylori (strain 26695)
Analyse Crystal structure of truncated flgd (monoclinic form) from the human pathogen… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5K5Y
- Type
- protein
- Length
- 584 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Basal-body rod modification protein flgd
- UniProt
- O25565
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Basal-body rod modification protein flgd | protein | 146 | 4% helix, 49% strand | O25565 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 679 | 0.65 | 0.74 | 57 | empty |
| 2 | 518 | 0.60 | 0.74 | 42 | empty |
| 3 | 52 | 0.26 | 0.74 | 13 | empty |
| 4 | 53 | 0.24 | 0.72 | 11 | empty |
Interfaces
3 interfaces between chains.
- A–B · 498 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 219 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 92 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5K5Y · Crystal structure of truncated FlgD (monoclinic form) from the human pathogen… · 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 O25565
- Elsewhere: RCSB PDB 5K5Y · PDBe 5K5Y · UniProt O25565
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