Research workbench
Crystal structure of the secreted protein HP1454 from the human pathogen helicobacter pylori
Analyse Crystal structure of the secreted protein HP1454 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
- 4KZS
- Type
- protein
- Length
- 242 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LPP20 lipofamily protein
- UniProt
- K2KM35
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LPP20 lipofamily protein | protein | 242 | 44% helix, 16% strand | K2KM35 |
Ligands and binding sites
- 1PE · Pentaethylene glycol · additive
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.69 | 0.93 | 20 | empty |
| 2 | 120 | 0.47 | 0.79 | 15 | empty |
Compared structures
- 4KZS · Crystal structure of the secreted protein HP1454 from the human pathogen Helicobacter… · 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 K2KM35
- Elsewhere: RCSB PDB 4KZS · PDBe 4KZS · UniProt K2KM35
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