Research workbench
Porcine kidney D-amino acid oxidase
Analyse Porcine kidney D-amino acid oxidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VE9
- Type
- protein
- Length
- 680 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-amino acid oxidase
- EC
- 1.4.3.3
- UniProt
- P00371
- Ligands
- FAD, BEZ
- Pockets
- 11 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | D-amino acid oxidase (EC 1.4.3.3) | protein | 340 | 32% helix, 28% strand | P00371 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- BEZ · Benzoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 399 | 0.84 | 0.93 | 53 | FAD, BEZ |
| 2 | 383 | 0.84 | 0.93 | 54 | FAD, BEZ |
| 3 | 68 | 0.72 | 0.96 | 18 | empty |
| 4 | 77 | 0.68 | 0.93 | 25 | empty |
| 5 | 71 | 0.50 | 0.85 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1570 Ų buried · 19 hydrogen bonds · protein-protein
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 P00371
- Elsewhere: RCSB PDB 1VE9 · PDBe 1VE9 · UniProt P00371
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