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Crystal structure of E114D mutant of CG10062 with a covalent intermediate of the hydration of acetylenecarboxylic acid
Analyse Crystal structure of E114D mutant of CG10062 with a covalent intermediate of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MS9
- Type
- protein
- Length
- 1,452 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-oxalocrotonate tautomerase
- EC
- 5.3.2.6
- UniProt
- A0A0S2T163
- Ligands
- 3OH, SO4
- Pockets
- 16 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | 4-oxalocrotonate tautomerase (EC 5.3.2.6) | protein | 121 | 40% helix, 31% strand | A0A0S2T163 |
Ligands and binding sites
- 3OH · 3-hydroxy-propanoic acid · ligand · 5 copies · chains A, C, B, F, G, H, I, J, K
- SO4 · Sulfate ion · ion · 7 copies · chains C, D, E, F, H, G, J, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 957 | 0.83 | 0.84 | 78 | empty |
| 2 | 133 | 0.81 | 0.98 | 21 | empty |
| 3 | 110 | 0.79 | 0.98 | 18 | empty |
| 4 | 95 | 0.78 | 0.98 | 20 | empty |
| 5 | 93 | 0.76 | 0.97 | 19 | empty |
Interfaces
23 interfaces between chains.
- K–L · 1414 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1402 Ų buried · 21 hydrogen bonds · protein-protein
- D–E · 1401 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 1392 Ų buried · 20 hydrogen bonds · protein-protein
- J–L · 1387 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 covalent (covalent ligand).
Compared structures
- 7MS9 · Crystal structure of E114D mutant of Cg10062 with a covalent intermediate of the… · 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 A0A0S2T163
- Elsewhere: RCSB PDB 7MS9 · PDBe 7MS9 · UniProt A0A0S2T163
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