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X-ray structure of catalytic domain of endolysin from clostridium perfringens phage PHISM101

Analyse X-ray structure of catalytic domain of endolysin from clostridium perfringens… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KRU
Type: protein
Length: 214 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Autolytic lysozyme
EC: 3.2.1.17
UniProt: Q0SPG7
Ligands: NDG, NAG, PO4
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Autolytic lysozyme (EC 3.2.1.17)	protein	214	31% helix, 25% strand	Q0SPG7

Ligands and binding sites

NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
PO4 · Phosphate ion · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	107	0.42	0.77	20	NDG

Compared structures

4KRU · X-ray structure of catalytic domain of endolysin from clostridium perfringens phage… · 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 Q0SPG7
Elsewhere: RCSB PDB 4KRU · PDBe 4KRU · UniProt Q0SPG7

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