Research workbench
Crystal structure of fumarylpyruvate hydrolase from corynebacterium glutamicum
Analyse Crystal structure of fumarylpyruvate hydrolase from corynebacterium glutamicum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J57
- Type
- protein
- Length
- 560 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Predicted 2-keto-4-pentenoate HYDRATASE/2-oxohepta-3-ene-1, 7-dioic acid hydratase
- UniProt
- A0A1R4GQY2
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Predicted 2-keto-4-pentenoate HYDRATASE/2-oxohepta-3-ene-1, 7-dioic acid hydratase | protein | 280 | 19% helix, 35% strand | A0A1R4GQY2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 9 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.59 | 0.78 | 37 | SO4 |
| 2 | 200 | 0.55 | 0.79 | 33 | SO4, GOL |
| 3 | 206 | 0.48 | 0.75 | 49 | empty |
Interfaces
1 interface between chains.
- A–B · 1734 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 6J57 · Crystal structure of fumarylpyruvate hydrolase from Corynebacterium glutamicum · 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 A0A1R4GQY2
- Elsewhere: RCSB PDB 6J57 · PDBe 6J57 · UniProt A0A1R4GQY2
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