Research workbench
Crystal structure of cuss histidine kinase catalytic core from escherichia COLI
Analyse Crystal structure of cuss histidine kinase catalytic core from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ZP0
- Type
- protein
- Length
- 1,300 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein
- EC
- 2.7.13.3
- UniProt
- A0A2J1D710
- Pockets
- 13 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Sensor protein (EC 2.7.13.3) | protein | 217 | 51% helix, 22% strand | A0A2J1D710 |
| E, F | Sensor protein (EC 2.7.13.3) | protein | 216 | 49% helix, 22% strand | A0A2J1D710 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains D, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1047 | 0.79 | 0.81 | 119 | empty |
| 2 | 596 | 0.73 | 0.81 | 60 | empty |
| 3 | 513 | 0.71 | 0.81 | 52 | empty |
| 4 | 287 | 0.71 | 0.85 | 53 | empty |
| 5 | 439 | 0.70 | 0.81 | 50 | empty |
Interfaces
9 interfaces between chains.
- C–D · 1711 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 1665 Ų buried · 2 hydrogen bonds · protein-protein
- E–F · 1482 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 1044 Ų buried · 12 hydrogen bonds · protein-protein
- C–E · 707 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 7ZP0 · Crystal structure of CusS histidine kinase catalytic core from Escherichia coli · 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 A0A2J1D710
- Elsewhere: RCSB PDB 7ZP0 · PDBe 7ZP0 · UniProt A0A2J1D710
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