Research workbench
E315Q mutant form of fumarase C from E.COLI
Analyse E315Q mutant form of fumarase C from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KQ7
- Type
- protein
- Length
- 911 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fumarate hydratase class II
- EC
- 4.2.1.2
- UniProt
- P05042
- Ligands
- MLT
- Pockets
- 6 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fumarate hydratase class II (EC 4.2.1.2) | protein | 456 | 60% helix, 8% strand | P05042 |
| B | Fumarate hydratase class II (EC 4.2.1.2) | protein | 455 | 61% helix, 8% strand | P05042 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.58 | 0.77 | 37 | empty |
| 2 | 210 | 0.52 | 0.77 | 31 | empty |
| 3 | 178 | 0.46 | 0.76 | 24 | empty |
| 4 | 75 | 0.36 | 0.76 | 14 | empty |
| 5 | 68 | 0.36 | 0.77 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2059 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
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 P05042
- Elsewhere: RCSB PDB 1KQ7 · PDBe 1KQ7 · UniProt P05042
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