Research workbench
Crystal structure of a 4-oxalocrotonate tautomerase mutant at 2.7 ångström
Analyse Crystal structure of a 4-oxalocrotonate tautomerase mutant at 2.7 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CLN
- Type
- protein
- Length
- 684 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-hydroxymuconate tautomerase
- EC
- 5.3.2.6
- UniProt
- Q01468
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 57 | 42% helix, 32% strand | Q01468 |
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 | 1190 | 0.79 | 0.81 | 80 | empty |
| 2 | 99 | 0.56 | 0.84 | 17 | empty |
| 3 | 75 | 0.54 | 0.86 | 16 | empty |
| 4 | 87 | 0.53 | 0.84 | 16 | empty |
| 5 | 111 | 0.50 | 0.81 | 21 | empty |
Interfaces
21 interfaces between chains.
- C–D · 909 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 897 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 890 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 590 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 572 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5CLN · Crystal structure of a 4-oxalocrotonate tautomerase mutant at 2.7 Angstrom · 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 5CLN · PDBe 5CLN · UniProt Q01468
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