Research workbench
Complex between bacterial chemotaxis histidine kinase chea domains P4 and P5 and receptor-adaptor protein chew
Analyse Complex between bacterial chemotaxis histidine kinase chea domains P4 and P5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CH4
- Type
- protein
- Length
- 904 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein chea; Chemotaxis protein chew
- EC
- 2.7.3.-
- UniProt
- Q56310, Q56311
- Ligands
- ANP
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 21% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis protein chea (EC 2.7.3.-) | protein | 320 | 24% helix, 34% strand | Q56310 |
| B | Chemotaxis protein chea (EC 2.7.3.-) | protein | 305 | 27% helix, 37% strand | Q56310 |
| W | Chemotaxis protein chew | protein | 139 | 10% helix, 42% strand | Q56311 |
| Y | Chemotaxis protein chew | protein | 140 | 12% helix, 44% strand | Q56311 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 935 | 0.80 | 0.82 | 108 | ANP |
| 2 | 968 | 0.77 | 0.79 | 85 | empty |
| 3 | 347 | 0.64 | 0.79 | 41 | empty |
| 4 | 182 | 0.59 | 0.81 | 27 | ANP |
| 5 | 120 | 0.37 | 0.73 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–W · 1204 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 1156 Ų buried · 15 hydrogen bonds · protein-protein
- B–Y · 875 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2CH4 · Complex between Bacterial Chemotaxis histidine kinase CheA domains P4 and P5 and… · the same entry in another collection · chain Y against Y, TM-score 1.00
- Q56311 · AlphaFold monomer V2.0 prediction for chemotaxis protein chew (Q56311) · a predicted model of the same protein · chain W against A, TM-score 0.95
- Q56310 · AlphaFold monomer V2.0 prediction for chemotaxis protein chea (Q56310) · a predicted model of the same protein · chain A against A, TM-score 0.59
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 Q56310
- Every structure of UniProt Q56311
- Elsewhere: RCSB PDB 2CH4 · PDBe 2CH4 · UniProt Q56310 · UniProt Q56311
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.