Research workbench
Crystal structure of recombinat mutant Q185R of human fumarase
Analyse Crystal structure of recombinat mutant Q185R of human fumarase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V8F
- Type
- protein
- Length
- 924 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fumarate hydratase, mitochondrial
- EC
- 4.2.1.2
- UniProt
- P07954
- Ligands
- SO4, CL
- Pockets
- 12 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fumarate hydratase, mitochondrial (EC 4.2.1.2) | protein | 462 | 61% helix, 8% strand | P07954 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
- CL · Chloride ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.58 | 0.89 | 22 | empty |
| 2 | 203 | 0.44 | 0.73 | 32 | empty |
| 3 | 58 | 0.42 | 0.82 | 15 | empty |
| 4 | 57 | 0.39 | 0.81 | 16 | empty |
| 5 | 131 | 0.39 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 3161 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 6V8F · Crystal structure of recombinat mutant Q185R of human fumarase · the same entry in another collection · chain A against A, TM-score 1.00
- P07954 · AlphaFold monomer V2.0 prediction for fumarate hydratase, mitochondrial (P07954) · a predicted model of the same protein · 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 P07954
- Elsewhere: RCSB PDB 6V8F · PDBe 6V8F · UniProt P07954
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