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Crystal structure of a enoyl-CoA hydratase from polaromonas sp. JS666

Analyse Crystal structure of a enoyl-CoA hydratase from polaromonas sp. JS666 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JFC
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-CoA hydratase
EC: 4.2.1.17
UniProt: Q129C0
Pockets: 4 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-CoA hydratase (EC 4.2.1.17)	protein	257	53% helix, 17% strand	Q129C0

Ligands and binding sites

GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	250	0.60	0.80	35	GOL
2	257	0.51	0.75	35	empty
3	63	0.35	0.78	18	empty
4	89	0.35	0.74	18	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

4JFC · Crystal structure of a enoyl-CoA hydratase from Polaromonas sp. JS666 · 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 Q129C0
Elsewhere: RCSB PDB 4JFC · PDBe 4JFC · UniProt Q129C0

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