Research workbench
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at PH6 at 293K (2)
Analyse Copper amine oxidase from arthrobacter globiformis anaerobically reduced by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZPH
- Type
- protein
- Length
- 1,240 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylethylamine oxidase
- EC
- 1.4.3.21
- UniProt
- P46881
- Ligands
- CU, NA
- Pockets
- 17 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phenylethylamine oxidase (EC 1.4.3.21) | protein | 620 | 13% helix, 43% strand | P46881 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1161 | 0.89 | 0.90 | 131 | empty |
| 2 | 315 | 0.72 | 0.85 | 56 | empty |
| 3 | 60 | 0.70 | 0.96 | 25 | empty |
| 4 | 316 | 0.66 | 0.81 | 38 | empty |
| 5 | 318 | 0.63 | 0.80 | 50 | empty |
Interfaces
1 interface between chains.
- A–B · 6956 Ų buried · 104 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 5ZPH · Copper amine oxidase from Arthrobacter globiformis anaerobically reduced by ethylamine at… · 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 P46881
- Elsewhere: RCSB PDB 5ZPH · PDBe 5ZPH · UniProt P46881
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