Research workbench
X-ray crystal structure of bacillus stearothermophilus histidine phosphocarrier protein (hpr) F29W mutant
Analyse X-ray crystal structure of bacillus stearothermophilus histidine phosphocarrier… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y51
- Type
- protein
- Length
- 261 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphocarrier protein hpr
- UniProt
- P42013
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Phosphocarrier protein hpr | protein | 87 | 37% helix, 28% strand | P42013 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.38 | 0.75 | 26 | empty |
| 2 | 52 | 0.25 | 0.73 | 13 | empty |
Interfaces
3 interfaces between chains.
- B–C · 372 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 285 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 30 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1Y51 · X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein… · the same entry in another collection · chain A against A, TM-score 1.00
- P42013 · AlphaFold monomer V2.0 prediction for phosphocarrier protein hpr (P42013) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P42013
- Elsewhere: RCSB PDB 1Y51 · PDBe 1Y51 · UniProt P42013
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