Research workbench
Crystal structure of protein LPP20 (HP1456) from helicobacter pylori
Analyse Crystal structure of protein LPP20 (HP1456) from helicobacter pylori in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OK8
- Type
- protein
- Length
- 457 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LPP20 lipoprotein
- UniProt
- P0A0V1
- Ligands
- CA
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | LPP20 lipoprotein | protein | 114 | 55% helix, 22% strand | P0A0V1 |
| B | LPP20 lipoprotein | protein | 115 | 55% helix, 22% strand | P0A0V1 |
Ligands and binding sites
- CA · Calcium ion · metal · chains B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 823 | 0.74 | 0.79 | 81 | EPE, CA |
| 2 | 59 | 0.36 | 0.79 | 14 | empty |
| 3 | 77 | 0.35 | 0.76 | 18 | empty |
| 4 | 88 | 0.34 | 0.74 | 14 | empty |
| 5 | 56 | 0.28 | 0.73 | 10 | empty |
Interfaces
4 interfaces between chains.
- C–D · 527 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 312 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 200 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 58 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 P0A0V1
- Elsewhere: RCSB PDB 5OK8 · PDBe 5OK8 · UniProt P0A0V1
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