Research workbench
Crystal structure of burkholderia pseudomallei effector protein chbp in complex with ubiquitin
Analyse Crystal structure of burkholderia pseudomallei effector protein chbp in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HCN
- Type
- protein
- Length
- 322 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative ATP/GTP binding protein; Polyubiquitin
- UniProt
- Q63KH5, P0CG63
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ATP/GTP binding protein | protein | 245 | 48% helix, 12% strand | Q63KH5 |
| B | Polyubiquitin | protein | 77 | 23% helix, 34% strand | P0CG63 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A, B
- FMT · Formic acid · additive · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A
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 | 63 | 0.71 | 0.97 | 19 | empty |
| 2 | 140 | 0.45 | 0.77 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1386 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 4HCN · Crystal structure of Burkholderia pseudomallei effector protein CHBP in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P0CG63 · AlphaFold monomer V2.0 prediction for polyubiquitin (P0CG63) · a predicted model of the same protein · chain B against A, TM-score 0.89
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 Q63KH5
- Every structure of UniProt P0CG63
- Elsewhere: RCSB PDB 4HCN · PDBe 4HCN · UniProt Q63KH5 · UniProt P0CG63
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