MolNFT v1 · #159169 · protein
Crystal structure of apo unfused 4-ot
6OGM · 4-oxalocrotonate tautomerase: “Crystal structure of apo unfused 4-ot”. X-ray diffraction, 8 pockets (best druggability 0.75). MolNFT v1 #159169 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6OGM
- Type
- protein
- Length
- 723 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-oxalocrotonate tautomerase
- UniProt
- Q392K7
- Pockets
- 8 · best druggability 0.75
Structure
x-ray diffraction · 6 distinct chains · 40% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G, L | 4-oxalocrotonate tautomerase | protein | 61 | 36% helix, 31% strand | Q392K7 |
| B, C, H | 4-oxalocrotonate tautomerase | protein | 58 | 43% helix, 33% strand | Q392K7 |
| D | 4-oxalocrotonate tautomerase | protein | 61 | 46% helix, 31% strand | Q392K7 |
| E | 4-oxalocrotonate tautomerase | protein | 63 | 35% helix, 30% strand | Q392K7 |
| F, K | 4-oxalocrotonate tautomerase | protein | 62 | 40% helix, 31% strand | Q392K7 |
| I, J | 4-oxalocrotonate tautomerase | protein | 59 | 42% helix, 32% strand | Q392K7 |
Ligands and binding sites
- FMT · Formic acid · additive · 6 copies · chains A, C, F, B, D, E, G, I, L, H, J, K
- GOL · Glycerol · additive · 2 copies · chains A, B, C, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.75 | 0.98 | 27 | empty |
| 2 | 63 | 0.72 | 0.97 | 25 | empty |
| 3 | 373 | 0.57 | 0.75 | 42 | GOL |
| 4 | 134 | 0.45 | 0.77 | 21 | empty |
| 5 | 105 | 0.44 | 0.78 | 20 | empty |
Interfaces
28 interfaces between chains.
- A–C · 992 Ų buried · 10 hydrogen bonds · protein-protein
- B–E · 987 Ų buried · 9 hydrogen bonds · protein-protein
- H–K · 982 Ų buried · 10 hydrogen bonds · protein-protein
- G–I · 971 Ų buried · 9 hydrogen bonds · protein-protein
- J–L · 937 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 covalent (additive adduct).
Compared structures
- 6OGM · Crystal structure of apo unFused 4-OT · 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 Q392K7
- Elsewhere: RCSB PDB 6OGM · PDBe 6OGM · UniProt Q392K7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.