Research workbench
Crystal structure of the native copper homeostasis protein (cutcm) with calcium binding from shigella flexneri 2A str. 301
Analyse Crystal structure of the native copper homeostasis protein (cutcm) with calcium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X7I
- Type
- protein
- Length
- 474 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper homeostasis protein cutc
- UniProt
- P67825
- Ligands
- CA
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper homeostasis protein cutc | protein | 236 | 41% helix, 21% strand | P67825 |
| B | Copper homeostasis protein cutc | protein | 238 | 41% helix, 20% strand | P67825 |
Ligands and binding sites
- CA · Calcium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.72 | 0.89 | 63 | empty |
| 2 | 138 | 0.58 | 0.84 | 30 | empty |
| 3 | 229 | 0.57 | 0.79 | 30 | empty |
| 4 | 318 | 0.57 | 0.76 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 1953 Ų buried · 41 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1X7I · Crystal structure of the native copper homeostasis protein (cutCm) with calcium binding… · the same entry in another collection · chain A against A, TM-score 1.00
- P67825 · AlphaFold monomer V2.0 prediction for copper homeostasis protein cutc (P67825) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P67825
- Elsewhere: RCSB PDB 1X7I · PDBe 1X7I · UniProt P67825
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