MolNFT v1 · #20432 · protein
L-amino acid oxidase from agkistrodon halys pallas
1REO · Ahplaao: “L-amino acid oxidase from agkistrodon halys pallas”. X-ray diffraction, 2 ligands (FAD, NAG), 2 pockets (best druggability 0.86). MolNFT v1 #20432 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1REO
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ahplaao
- EC
- 1.4.3.2
- UniProt
- Q6STF1
- Ligands
- FAD, NAG
- Pockets
- 2 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ahplaao (EC 1.4.3.2) | protein | 484 | 42% helix, 22% strand | Q6STF1 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1136 | 0.86 | 0.87 | 126 | CIT, FAD |
| 2 | 179 | 0.55 | 0.80 | 31 | empty |
Modifications
Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).
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 Q6STF1
- Elsewhere: RCSB PDB 1REO · PDBe 1REO · UniProt Q6STF1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.