Research workbench
Copper chaperone ATX1 from synechocystis PCC6803 (CU1, trimeric form, HIS61TYR mutant)
Analyse Copper chaperone ATX1 from synechocystis PCC6803 (CU1, trimeric form, HIS61TYR… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XMV
- Type
- protein
- Length
- 378 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SSR2857 protein
- UniProt
- P73213
- Ligands
- CU1
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | SSR2857 protein | protein | 63 | 38% helix, 22% strand | P73213 |
Ligands and binding sites
- CU1 · Copper (I) ion · metal · 8 copies · chains A, C, B, D, F, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 824 | 0.80 | 0.83 | 104 | CU1 |
| 2 | 101 | 0.35 | 0.74 | 21 | empty |
| 3 | 70 | 0.29 | 0.73 | 20 | empty |
Interfaces
12 interfaces between chains.
- B–E · 270 Ų buried · 4 hydrogen bonds · protein-protein
- A–F · 266 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 258 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 181 Ų buried · 1 hydrogen bond · protein-protein
- D–E · 168 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2XMV · Copper chaperone Atx1 from Synechocystis PCC6803 (Cu1, trimeric form, His61Tyr mutant) · 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 P73213
- Elsewhere: RCSB PDB 2XMV · PDBe 2XMV · UniProt P73213
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