MolNFT v1 · #89470 · protein

Structural investigation of bacteriophage PHI6 lysin (wt)

4DQ5 · Membrane protein PHI6 P5WT: “Structural investigation of bacteriophage PHI6 lysin (wt)”. X-ray diffraction, 1 ligand (AES), 1 pocket (best druggability 0.82). MolNFT v1 #89470 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4DQ5
Type: protein
Length: 324 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Membrane protein PHI6 P5WT
UniProt: Q283U5
Ligands: AES
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 P5WT	protein	164	59% helix, 9% strand	Q283U5
B	Membrane protein PHI6 P5WT	protein	160	62% helix, 11% strand	Q283U5

Ligands and binding sites

AES · 4-(2-aminoethyl)benzenesulfonyl fluoride · ligand · 2 copies · chains A, B

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	1019	0.82	0.83	81	AES

Interfaces

1 interface between chains.

A–B · 762 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4DQ5 · Structural Investigation of Bacteriophage Phi6 Lysin (WT) · 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 4DQ5 · PDBe 4DQ5 · UniProt Q283U5

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