MolNFT v1 · #37235 · protein
Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site
2FUS · Fumarase C: “Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site”. X-ray diffraction, 5 pockets (best druggability 0.58). MolNFT v1 #37235 on GenesisL1: 3D structure, binding…
- PDB
- 2FUS
- 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
- Pockets
- 5 · best druggability 0.58
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
- 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 308 | 0.58 | 0.77 | 41 | empty |
| 2 | 190 | 0.47 | 0.76 | 28 | empty |
| 3 | 161 | 0.47 | 0.77 | 21 | empty |
| 4 | 60 | 0.30 | 0.74 | 11 | empty |
| 5 | 54 | 0.30 | 0.75 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 2030 Ų buried · 45 hydrogen bonds · protein-protein
Compared structures
- 2FUS · Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic… · the same entry in another collection · chain A against A, TM-score 1.00
- P05042 · AlphaFold monomer V2.0 prediction for fumarate hydratase class II (P05042) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 2FUS · PDBe 2FUS · UniProt P05042
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