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Crystal structure of E. COLI clpb
Analyse Crystal structure of E. COLI clpb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CIU
- Type
- protein
- Length
- 657 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein clpb
- UniProt
- P63284
- Ligands
- ADP
- Pockets
- 8 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 60% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein clpb | protein | 657 | 60% helix, 13% strand | P63284 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 633 | 0.67 | 0.76 | 60 | empty |
| 2 | 267 | 0.60 | 0.80 | 33 | ADP |
| 3 | 184 | 0.52 | 0.78 | 25 | ADP |
| 4 | 179 | 0.48 | 0.76 | 24 | empty |
| 5 | 91 | 0.47 | 0.81 | 16 | empty |
Modifications
Observed in the structure: 17 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 P63284
- Elsewhere: RCSB PDB 4CIU · PDBe 4CIU · UniProt P63284
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