Research workbench
Crystal structure of histidine-containing phosphotransfer protein, ZMHP2, from maize
Analyse Crystal structure of histidine-containing phosphotransfer protein, ZMHP2, from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WN0
- Type
- protein
- Length
- 531 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidine-containing phosphotransfer protein
- UniProt
- Q9SLX1
- Pockets
- 6 · best druggability 0.53
Structure
x-ray diffraction · 3 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine-containing phosphotransfer protein | protein | 131 | 79% helix, 0% strand | Q9SLX1 |
| B | Histidine-containing phosphotransfer protein | protein | 124 | 80% helix, 0% strand | Q9SLX1 |
| C, D | Histidine-containing phosphotransfer protein | protein | 138 | 83% helix, 0% strand | Q9SLX1 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.53 | 0.74 | 32 | empty |
| 2 | 225 | 0.50 | 0.76 | 24 | empty |
| 3 | 126 | 0.37 | 0.73 | 23 | empty |
| 4 | 53 | 0.34 | 0.79 | 13 | empty |
| 5 | 55 | 0.31 | 0.76 | 14 | empty |
Interfaces
4 interfaces between chains.
- B–C · 753 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 740 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 182 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 147 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1WN0 · Crystal Structure of Histidine-containing Phosphotransfer Protein, ZmHP2, from maize · 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 Q9SLX1
- Elsewhere: RCSB PDB 1WN0 · PDBe 1WN0 · UniProt Q9SLX1
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