Research workbench
Crystal structure of putative copper homeostasis protein cutc from bacillus anthracis
Analyse Crystal structure of putative copper homeostasis protein cutc from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R9X
- Type
- protein
- Length
- 450 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper homeostasis protein cutc
- UniProt
- Q81NS5
- Ligands
- CA
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Copper homeostasis protein cutc | protein | 225 | 40% helix, 17% strand | Q81NS5 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A, B
- PGE · Triethylene glycol · additive · chains A
- GOL · Glycerol · additive · chains B
- EDO · 1,2-ethanediol · additive · chains 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 | 324 | 0.59 | 0.77 | 36 | empty |
| 2 | 150 | 0.50 | 0.79 | 25 | GOL |
| 3 | 52 | 0.34 | 0.79 | 17 | empty |
| 4 | 69 | 0.33 | 0.76 | 20 | PGE |
| 5 | 69 | 0.33 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 406 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 4R9X · Crystal Structure of Putative Copper Homeostasis Protein CutC from Bacillus anthracis · 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 Q81NS5
- Elsewhere: RCSB PDB 4R9X · PDBe 4R9X · UniProt Q81NS5
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