Research workbench
The crystal structure of human enoyl-coenzyme a (CoA) hydratase short chain 1, ECHS1
Analyse The crystal structure of human enoyl-coenzyme a (CoA) hydratase short chain 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HW5
- Type
- protein
- Length
- 1,560 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-CoA hydratase
- EC
- 4.2.1.17
- UniProt
- P30084
- Ligands
- COO, MG
- Pockets
- 14 · best druggability 0.90
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Enoyl-CoA hydratase (EC 4.2.1.17) | protein | 260 | 50% helix, 16% strand | P30084 |
Ligands and binding sites
- COO · Crotonyl coenzyme A · ligand · 2 copies · chains B, C
- MG · Magnesium ion · metal · 4 copies · chains C, D, A, F, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 932 | 0.90 | 0.92 | 122 | MG |
| 2 | 1011 | 0.83 | 0.84 | 127 | empty |
| 3 | 299 | 0.77 | 0.88 | 60 | empty |
| 4 | 230 | 0.75 | 0.89 | 37 | empty |
| 5 | 108 | 0.69 | 0.91 | 30 | empty |
Interfaces
15 interfaces between chains.
- A–D · 2238 Ų buried · 32 hydrogen bonds · protein-protein
- A–F · 2173 Ų buried · 30 hydrogen bonds · protein-protein
- B–E · 2173 Ų buried · 31 hydrogen bonds · protein-protein
- B–C · 2160 Ų buried · 32 hydrogen bonds · protein-protein
- C–E · 2153 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 2HW5 · The crystal structure of human enoyl-coenzyme A (CoA) hydratase short chain 1, ECHS1 · the same entry in another collection · chain E against E, TM-score 1.00
- P30084 · AlphaFold monomer V2.0 prediction for enoyl-CoA hydratase, mitochondrial (P30084) · a predicted model of the same protein · chain C 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 P30084
- Elsewhere: RCSB PDB 2HW5 · PDBe 2HW5 · UniProt P30084
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