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Crystal structure of human fumarate hydratase
Analyse Crystal structure of human fumarate hydratase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E04
- Type
- protein
- Length
- 1,783 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fumarate hydratase
- EC
- 4.2.1.2
- UniProt
- P07954
- Pockets
- 16 · best druggability 0.76
Structure
x-ray diffraction · 4 distinct chains · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fumarate hydratase (EC 4.2.1.2) | protein | 456 | 62% helix, 8% strand | P07954 |
| B | Fumarate hydratase (EC 4.2.1.2) | protein | 454 | 61% helix, 7% strand | P07954 |
| C | Fumarate hydratase (EC 4.2.1.2) | protein | 415 | 58% helix, 9% strand | P07954 |
| D | Fumarate hydratase (EC 4.2.1.2) | protein | 458 | 62% helix, 8% strand | P07954 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 426 | 0.76 | 0.85 | 48 | empty |
| 2 | 485 | 0.75 | 0.83 | 57 | empty |
| 3 | 549 | 0.73 | 0.81 | 50 | empty |
| 4 | 502 | 0.69 | 0.80 | 67 | empty |
| 5 | 65 | 0.69 | 0.96 | 17 | empty |
Interfaces
6 interfaces between chains.
- A–D · 3122 Ų buried · 41 hydrogen bonds · protein-protein
- B–C · 3093 Ų buried · 39 hydrogen bonds · protein-protein
- A–B · 2502 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 2421 Ų buried · 23 hydrogen bonds · protein-protein
- B–D · 1979 Ų buried · 47 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 P07954
- Elsewhere: RCSB PDB 3E04 · PDBe 3E04 · UniProt P07954
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