MolNFT v1 · #77163 · protein
Crystal structure of an enoyl-CoA hydratase (ECHA3) from mycobacterium marinum
3R6H · Enoyl-CoA hydratase, ECHA3: “Crystal structure of an enoyl-CoA hydratase (ECHA3) from mycobacterium marinum”. X-ray diffraction, 2 ligands (K, CL), 1 pocket (best druggability 0.48). MolNFT v1 #77163 on GenesisL1: 3D structure…
- PDB
- 3R6H
- Type
- protein
- Length
- 225 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enoyl-CoA hydratase, ECHA3
- UniProt
- B2HSG1
- Ligands
- K, CL
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enoyl-CoA hydratase, ECHA3 | protein | 225 | 52% helix, 17% strand | B2HSG1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.48 | 0.79 | 28 | K, CL |
Compared structures
- 3R6H · Crystal structure of an enoyl-CoA hydratase (ECHA3) from Mycobacterium marinum · the same entry in another collection · chain A 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 B2HSG1
- Elsewhere: RCSB PDB 3R6H · PDBe 3R6H · UniProt B2HSG1
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