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Crystal structure of glpg at 1.9A resolution

Analyse Crystal structure of glpg at 1.9A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3B45
Type: protein
Length: 180 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glpg
UniProt: P09391
Ligands: BNG
Pockets: 3 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glpg	protein	180	76% helix, 0% strand	P09391

Ligands and binding sites

BNG · nonyl beta-D-glucopyranoside · ligand · 17 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.36	0.78	12	empty
2	68	0.34	0.75	15	BNG
3	56	0.30	0.75	14	empty

Compared structures

3B45 · Crystal structure of GlpG at 1.9A resolution · the same entry in another collection · chain A against A, TM-score 1.00
P09391 · AlphaFold monomer V2.0 prediction for rhomboid protease glpg (P09391) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P09391
Elsewhere: RCSB PDB 3B45 · PDBe 3B45 · UniProt P09391

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