Research workbench

Crystal structure of a putative enoyl-CoA hydratase from novosphingobium aromaticivorans dsm 12444

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

PDB: 4OG1
Type: protein
Length: 257 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-CoA HYDRATASE/ISOMERASE
EC: 4.2.1.17
UniProt: Q2GB23
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-CoA HYDRATASE/ISOMERASE (EC 4.2.1.17)	protein	257	45% helix, 18% strand	Q2GB23

Ligands and binding sites

PE8 · 3,6,9,12,15,18,21-heptaoxatricosane-1,23-diol · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	117	0.40	0.75	27	empty
2	130	0.39	0.74	23	empty

Compared structures

4OG1 · Crystal Structure of a Putative Enoyl-CoA Hydratase from Novosphingobium aromaticivorans… · 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 Q2GB23
Elsewhere: RCSB PDB 4OG1 · PDBe 4OG1 · UniProt Q2GB23

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.