Research workbench
Crystal structure of cu-form czce from C. metallidurans CH34
Analyse Crystal structure of cu-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
- 2WTP
- Type
- protein
- Length
- 182 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ORF131 protein
- UniProt
- Q58AL9
- Ligands
- CU, MG, CL
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 21% 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 | 89 | 21% helix, 40% strand | Q58AL9 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 3 copies · chains A, B
- MG · Magnesium ion · metal · chains A, B
- CL · Chloride ion · ion · 10 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.60 | 0.83 | 23 | CL |
| 2 | 54 | 0.40 | 0.82 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 530 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2WTP · Crystal Structure of Cu-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 2WTP · PDBe 2WTP · UniProt Q58AL9
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