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Crystal structure of putative dienelactone hydrolase from klebsiella pneumoniae subsp. pneumoniae mgh 78578

Analyse Crystal structure of putative dienelactone hydrolase from klebsiella pneumoniae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3F67
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative dienelactone hydrolase
EC: 3.1.1.-
UniProt: A6TGL0
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative dienelactone hydrolase (EC 3.1.1.-)	protein	240	36% helix, 25% strand	A6TGL0

Ligands and binding sites

FMT · Formic acid · additive · 2 copies · chains A
EDO · 1,2-ethanediol · additive · chains A
ACY · Acetic acid · additive · 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	181	0.51	0.78	28	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

3F67 · Crystal Structure of Putative Dienelactone Hydrolase from Klebsiella pneumoniae subsp.… · 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 A6TGL0
Elsewhere: RCSB PDB 3F67 · PDBe 3F67 · UniProt A6TGL0

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