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The crystal structure of the hpt domain from the hpt sensor hybrid histidine kinase from shewanella to 1.80A
Analyse The crystal structure of the hpt domain from the hpt sensor hybrid histidine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MYF
- Type
- protein
- Length
- 461 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein
- EC
- 2.7.13.3
- UniProt
- A1RHE3
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sensor protein (EC 2.7.13.3) | protein | 117 | 80% helix, 0% strand | A1RHE3 |
| B, C | Sensor protein (EC 2.7.13.3) | protein | 114 | 80% helix, 0% strand | A1RHE3 |
| D | Sensor protein (EC 2.7.13.3) | protein | 116 | 80% helix, 0% strand | A1RHE3 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1173 | 0.81 | 0.82 | 106 | empty |
Interfaces
5 interfaces between chains.
- A–B · 724 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 724 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 313 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 86 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 54 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3MYF · The Crystal Structure of the HPT domain from the Hpt Sensor Hybrid Histidine Kinase from… · the same entry in another collection · chain D against D, 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 A1RHE3
- Elsewhere: RCSB PDB 3MYF · PDBe 3MYF · UniProt A1RHE3
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