Research workbench
Fumarase with bound 3-trimethylsilylsuccinic acid
Analyse Fumarase with bound 3-trimethylsilylsuccinic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FUQ
- Type
- protein
- Length
- 911 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fumarase C
- EC
- 4.2.1.2
- UniProt
- P05042
- Ligands
- SIF
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fumarase C (EC 4.2.1.2) | protein | 456 | 61% helix, 8% strand | P05042 |
| B | Fumarase C (EC 4.2.1.2) | protein | 455 | 62% helix, 8% strand | P05042 |
Ligands and binding sites
- SIF · 3-trimethylsilylsuccinic acid · ligand · 2 copies · chains A, B
- CIT · Citric acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 316 | 0.57 | 0.76 | 37 | empty |
| 2 | 235 | 0.50 | 0.76 | 31 | empty |
| 3 | 149 | 0.47 | 0.77 | 22 | empty |
| 4 | 60 | 0.29 | 0.74 | 12 | empty |
| 5 | 51 | 0.29 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 2036 Ų buried · 44 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 1FUQ · PDBe 1FUQ · UniProt P05042
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