Research workbench
Crystal structure of cpxahdc (trigonal form)
Analyse Crystal structure of cpxahdc (trigonal form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BIV
- Type
- protein
- Length
- 538 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sensor protein cpxa
- EC
- 2.7.13.3
- UniProt
- P0AE82
- Ligands
- ATP
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Sensor protein cpxa (EC 2.7.13.3) | protein | 269 | 56% helix, 15% strand | P0AE82 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 761 | 0.78 | 0.82 | 71 | empty |
| 2 | 183 | 0.74 | 0.91 | 33 | ATP |
| 3 | 309 | 0.72 | 0.85 | 48 | ATP |
| 4 | 62 | 0.51 | 0.86 | 16 | empty |
| 5 | 127 | 0.39 | 0.74 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 3779 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
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 P0AE82
- Elsewhere: RCSB PDB 4BIV · PDBe 4BIV · UniProt P0AE82
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