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The crystal structure of the putative cell surface hydrolase from lactobacillus plantarum WCFS1

Analyse The crystal structure of the putative cell surface hydrolase from lactobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LP5
Type: protein
Length: 250 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative cell surface hydrolase
UniProt: Q88XN2
Ligands: NA
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative cell surface hydrolase	protein	250	38% helix, 20% strand	Q88XN2

Ligands and binding sites

NA · Sodium ion · metal · 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	115	0.53	0.82	23	empty

Compared structures

3LP5 · The crystal structure of the putative cell surface hydrolase from Lactobacillus plantarum… · 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 Q88XN2
Elsewhere: RCSB PDB 3LP5 · PDBe 3LP5 · UniProt Q88XN2

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