Research workbench
Edta treated E. COLI copper amine oxidase
Analyse Edta treated E. COLI copper amine oxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WOF
- Type
- protein
- Length
- 1,438 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Primary amine oxidase
- EC
- 1.4.3.6
- UniProt
- P46883
- Ligands
- NA, CU
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Primary amine oxidase (EC 1.4.3.6) | protein | 718 | 12% helix, 44% strand | P46883 |
| B | Primary amine oxidase (EC 1.4.3.6) | protein | 720 | 13% helix, 44% strand | P46883 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A, B
- CU · Copper (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 725 | 0.87 | 0.91 | 72 | empty |
| 2 | 381 | 0.74 | 0.85 | 68 | empty |
| 3 | 281 | 0.74 | 0.87 | 57 | empty |
| 4 | 321 | 0.66 | 0.81 | 37 | empty |
| 5 | 325 | 0.64 | 0.80 | 51 | empty |
Interfaces
1 interface between chains.
- A–B · 7185 Ų buried · 136 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
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 P46883
- Elsewhere: RCSB PDB 2WOF · PDBe 2WOF · UniProt P46883
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