Research workbench
Crystal structure of apo-form czce from C. metallidurans CH34
Analyse Crystal structure of apo-form czce from C. metallidurans CH34 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WTO
- Type
- protein
- Length
- 184 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ORF131 protein
- UniProt
- Q58AL9
- Ligands
- MG, CL
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ORF131 protein | protein | 93 | 22% helix, 37% strand | Q58AL9 |
| B | ORF131 protein | protein | 91 | 23% helix, 38% strand | Q58AL9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.61 | 0.84 | 23 | CL |
Interfaces
1 interface between chains.
- A–B · 607 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 2WTO · Crystal Structure of Apo-form Czce from C. metallidurans CH34 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q58AL9
- Elsewhere: RCSB PDB 2WTO · PDBe 2WTO · UniProt Q58AL9
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