Research workbench
Structure of chea domain P4 in complex with adpcp and manganese
Analyse Structure of chea domain P4 in complex with adpcp and manganese in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I5A
- Type
- protein
- Length
- 358 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemotaxis protein chea
- EC
- 2.7.3.-
- UniProt
- Q56310
- Ligands
- ACP, MN
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemotaxis protein chea (EC 2.7.3.-) | protein | 181 | 42% helix, 25% strand | Q56310 |
| B | Chemotaxis protein chea (EC 2.7.3.-) | protein | 177 | 42% helix, 26% strand | Q56310 |
Ligands and binding sites
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · 2 copies · chains A, B
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.68 | 0.83 | 26 | MN, ACP |
| 2 | 381 | 0.66 | 0.80 | 48 | MN, ACP |
| 3 | 109 | 0.40 | 0.76 | 18 | empty |
| 4 | 66 | 0.35 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 410 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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
- Elsewhere: RCSB PDB 1I5A · PDBe 1I5A · UniProt Q56310
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