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Crystal structure of enoyl-CoA hydrotase from Deinococcus radiodurans R1

Analyse Crystal structure of enoyl-CoA hydrotase from Deinococcus radiodurans R1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4JOT
Type: protein
Length: 255 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.94
Source: Deinococcus radiodurans
Molecule: Enoyl-CoA hydratase, putative
UniProt: Q9RY37
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · resolution 1.94 · 1 distinct chain · 51% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-CoA hydratase, putative	protein	255	51% helix, 19% strand	Q9RY37

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	126	0.53	0.81	24	empty
2	148	0.43	0.75	19	empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

4JOT · Crystal structure of enoyl-CoA hydrotase from deinococcus radiodurans R1 · 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 Q9RY37
Elsewhere: RCSB PDB 4JOT · PDBe 4JOT · UniProt Q9RY37

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