MolNFT v1 · #91777 · protein

Crystal structure of the mtb enoyl CoA isomerase in complex with hydroxyhexanoyl CoA

4FND · Enoyl-CoA HYDRATASE/ISOMERASE family protein: “Crystal structure of the mtb enoyl CoA isomerase in complex with hydroxyhexanoyl CoA”. X-ray diffraction, 2 ligands (3H9, SO4), 1 pocket (best druggability 0.60). MolNFT v1 #91777 on…

PDB: 4FND
Type: protein
Length: 232 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-CoA HYDRATASE/ISOMERASE family protein
EC: 4.2.1.17
UniProt: P96907
Ligands: 3H9, SO4
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-CoA HYDRATASE/ISOMERASE family protein (EC 4.2.1.17)	protein	232	50% helix, 16% strand	P96907

Ligands and binding sites

3H9 · (S)-3-Hydroxyhexanoyl-CoA · ligand · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	144	0.60	0.83	25	empty

Compared structures

4FND · Crystal structure of the Mtb enoyl CoA isomerase in complex with hydroxyhexanoyl CoA · 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 P96907
Elsewhere: RCSB PDB 4FND · PDBe 4FND · UniProt P96907

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