MolNFT v1 · #26576 · protein

Crystal structure of GP5-S351L mutant and GP27 complex

1WTH · Tail-associated lysozyme: “Crystal structure of GP5-S351L mutant and GP27 complex”. X-ray diffraction, 2 ligands (K, PO4), 11 pockets (best druggability 0.72). MolNFT v1 #26576 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1WTH
Type: protein
Length: 932 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tail-associated lysozyme; Baseplate structural protein GP27
EC: 3.2.1.17
UniProt: P16009, P17172
Ligands: K, PO4
Pockets: 11 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 19% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Tail-associated lysozyme (EC 3.2.1.17)	protein	571	21% helix, 14% strand	P16009
D	Baseplate structural protein GP27	protein	361	17% helix, 37% strand	P17172

Ligands and binding sites

K · Potassium ion · metal · chains A
PO4 · Phosphate ion · ion · chains A

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

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	478	0.72	0.82	59	empty
2	359	0.66	0.80	42	empty
3	151	0.57	0.82	22	empty
4	86	0.51	0.83	18	empty
5	152	0.47	0.77	22	empty

Interfaces

1 interface between chains.

A–D · 1027 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1WTH · Crystal structure of gp5-S351L mutant and gp27 complex · 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 P16009
Every structure of UniProt P17172
Elsewhere: RCSB PDB 1WTH · PDBe 1WTH · UniProt P16009 · UniProt P17172

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