Research workbench
Bacillus amyloliquefaciens CBM33 in complex with CU(I) after photoreduction
Analyse Bacillus amyloliquefaciens CBM33 in complex with CU(I) after photoreduction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YOX
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RBAM17540
- EC
- 1.-.-.-
- UniProt
- E1UUV3
- Ligands
- CU1
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | RBAM17540 (EC 1.-.-.-) | protein | 178 | 22% helix, 38% strand | E1UUV3 |
Ligands and binding sites
- CU1 · Copper (I) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 388 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 2YOX · Bacillus amyloliquefaciens CBM33 in complex with Cu(I) after photoreduction · 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 E1UUV3
- Elsewhere: RCSB PDB 2YOX · PDBe 2YOX · UniProt E1UUV3
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