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4-oxalocrotonate tautomerase observed as an octodecamer, rhombohedral crystal form
Analyse 4-oxalocrotonate tautomerase observed as an octodecamer, rhombohedral crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OTB
- Type
- protein
- Length
- 707 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-oxalocrotonate tautomerase
- EC
- 5.3.2.-
- UniProt
- Q01468
- Pockets
- 11 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K | 4-oxalocrotonate tautomerase (EC 5.3.2.-) | protein | 59 | 42% helix, 31% strand | Q01468 |
| L | 4-oxalocrotonate tautomerase (EC 5.3.2.-) | protein | 58 | 38% helix, 31% strand | Q01468 |
Pockets
11 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.35 | 0.75 | 19 | empty |
| 2 | 76 | 0.34 | 0.75 | 17 | empty |
| 3 | 72 | 0.34 | 0.75 | 15 | empty |
| 4 | 60 | 0.33 | 0.76 | 12 | empty |
| 5 | 65 | 0.33 | 0.75 | 16 | empty |
Interfaces
10 interfaces between chains.
- E–F · 871 Ų buried · 10 hydrogen bonds · protein-protein
- K–L · 869 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 866 Ų buried · 10 hydrogen bonds · protein-protein
- G–H · 866 Ų buried · 8 hydrogen bonds · protein-protein
- I–J · 863 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4OTB · 4-oxalocrotonate tautomerase observed as an octodecamer, rhombohedral crystal form · the same entry in another collection · chain L against L, 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 Q01468
- Elsewhere: RCSB PDB 4OTB · PDBe 4OTB · UniProt Q01468
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