Research workbench
Crystal structure of a 4-oxalocrotonate tautomerase mutant in complex with nitrostyrene at 2.3 ångström
Analyse Crystal structure of a 4-oxalocrotonate tautomerase mutant in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CLO
- Type
- protein
- Length
- 1,025 residues
- Chains
- 18
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-hydroxymuconate tautomerase
- EC
- 5.3.2.6
- UniProt
- Q01468
- Ligands
- NS8
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 5 distinct chains · 44% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F, G, H, I, K, M, N, O, P, R | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 57 | 44% helix, 32% strand | Q01468 |
| C | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 54 | 46% helix, 31% strand | Q01468 |
| J | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 58 | 43% helix, 33% strand | Q01468 |
| L | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 59 | 42% helix, 31% strand | Q01468 |
| Q | 2-hydroxymuconate tautomerase (EC 5.3.2.6) | protein | 56 | 45% helix, 30% strand | Q01468 |
Ligands and binding sites
- NS8 · trans beta nitrostyrene · ligand · chains M, N, O
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 548 | 0.75 | 0.83 | 48 | empty |
| 2 | 276 | 0.62 | 0.80 | 37 | empty |
| 3 | 80 | 0.59 | 0.88 | 18 | empty |
| 4 | 71 | 0.58 | 0.89 | 17 | empty |
| 5 | 97 | 0.58 | 0.86 | 19 | NS8 |
Interfaces
44 interfaces between chains.
- C–D · 921 Ų buried · 16 hydrogen bonds · protein-protein
- G–H · 911 Ų buried · 16 hydrogen bonds · protein-protein
- O–P · 911 Ų buried · 15 hydrogen bonds · protein-protein
- Q–R · 902 Ų buried · 12 hydrogen bonds · protein-protein
- M–N · 894 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 5CLO · Crystal structure of a 4-oxalocrotonate tautomerase mutant in complex with nitrostyrene… · the same entry in another collection · chain K against K, 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 5CLO · PDBe 5CLO · UniProt Q01468
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