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Crystal structure of an enoyl-CoA HYDRATASE/ISOMERASE family protein from psudomonas syringae

Analyse Crystal structure of an enoyl-CoA HYDRATASE/ISOMERASE family protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OT6
Type: protein
Length: 230 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Enoyl-CoA HYDRATASE/ISOMERASE family protein
UniProt: Q884M3
Pockets: 2 · best druggability 0.53

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Enoyl-CoA HYDRATASE/ISOMERASE family protein	protein	230	51% helix, 19% strand	Q884M3

Ligands and binding sites

MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
MRD · (4R)-2-methylpentane-2,4-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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	99	0.53	0.83	19	MRD
2	74	0.34	0.76	21	empty

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

3OT6 · Crystal Structure of an enoyl-CoA hydratase/isomerase family protein from Psudomonas… · 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 Q884M3
Elsewhere: RCSB PDB 3OT6 · PDBe 3OT6 · UniProt Q884M3

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