Research workbench
Complex of thio (glycine oxidase) with acetyl-glycine
Analyse Complex of thio (glycine oxidase) with acetyl-glycine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NG3
- Type
- protein
- Length
- 728 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycine oxidase
- EC
- 1.5.3.-
- UniProt
- O31616
- Ligands
- FAD, AAC, PO4
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glycine oxidase (EC 1.5.3.-) | protein | 364 | 32% helix, 27% strand | O31616 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- AAC · Acetylamino-acetic acid · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 651 | 0.81 | 0.86 | 83 | FAD, AAC |
| 2 | 332 | 0.81 | 0.91 | 61 | FAD, AAC |
| 3 | 587 | 0.72 | 0.80 | 47 | PO4 |
| 4 | 172 | 0.57 | 0.81 | 36 | empty |
| 5 | 158 | 0.55 | 0.80 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 941 Ų buried · 12 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 O31616
- Elsewhere: RCSB PDB 1NG3 · PDBe 1NG3 · UniProt O31616
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