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Crystal structure of a putative hydrolase (LPG1103) from legionella pneumophila subsp. pneumophila str. philadelphia 1 at 1.15 a resolution

Analyse Crystal structure of a putative hydrolase (LPG1103) from legionella pneumophila… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EZI
Type: protein
Length: 371 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q5ZWI2
Ligands: CL
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	371	43% helix, 19% strand	Q5ZWI2

Ligands and binding sites

CL · Chloride ion · ion · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.74	0.98	17	PEG
2	339	0.63	0.79	30	empty
3	75	0.39	0.78	18	empty

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

4EZI · Crystal structure of a putative hydrolase (lpg1103) from Legionella pneumophila subsp.… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5ZWI2
Elsewhere: RCSB PDB 4EZI · PDBe 4EZI · UniProt Q5ZWI2

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