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Structural investigation of bacteriophage PHI6 lysin (V207F mutant)

Analyse Structural investigation of bacteriophage PHI6 lysin (V207F mutant) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4DQ7
Type: protein
Length: 328 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Membrane protein PHI6 P5
UniProt: Q283U5
Pockets: 1 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 60% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Membrane protein PHI6 P5	protein	168	57% helix, 9% strand	Q283U5
B	Membrane protein PHI6 P5	protein	160	63% helix, 11% strand	Q283U5

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	1189	0.82	0.83	100	empty

Interfaces

1 interface between chains.

A–B · 785 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4DQ7 · Structural Investigation of Bacteriophage Phi6 Lysin (V207F mutant) · 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 Q283U5
Elsewhere: RCSB PDB 4DQ7 · PDBe 4DQ7 · UniProt Q283U5

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