Research workbench
The CAP/CRP variant T127L/S128A
Analyse The CAP/CRP variant T127L/S128A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HW5
- Type
- protein
- Length
- 413 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catabolite gene activator
- UniProt
- P0ACJ8
- Ligands
- CMP
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catabolite gene activator | protein | 208 | 38% helix, 27% strand | P0ACJ8 |
| B | Catabolite gene activator | protein | 205 | 40% helix, 28% strand | P0ACJ8 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 582 | 0.76 | 0.83 | 69 | CMP |
| 2 | 506 | 0.74 | 0.82 | 66 | CMP |
| 3 | 62 | 0.32 | 0.76 | 14 | empty |
| 4 | 80 | 0.31 | 0.73 | 18 | empty |
| 5 | 53 | 0.30 | 0.76 | 13 | CMP |
Interfaces
1 interface between chains.
- A–B · 1606 Ų buried · 9 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 P0ACJ8
- Elsewhere: RCSB PDB 1HW5 · PDBe 1HW5 · UniProt P0ACJ8
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