Research workbench
Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at pH 6 at 283 K (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
- 5ZPA
- 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
- Pockets
- 16 · 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
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1042 | 0.89 | 0.91 | 136 | empty |
| 2 | 371 | 0.71 | 0.83 | 56 | empty |
| 3 | 355 | 0.67 | 0.81 | 56 | empty |
| 4 | 300 | 0.65 | 0.81 | 39 | empty |
| 5 | 305 | 0.64 | 0.81 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 6905 Ų buried · 103 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 5ZPA · 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 5ZPA · PDBe 5ZPA · UniProt P46881
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