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Crystal structure of E.COLI glpg at pH 4.5

Analyse Crystal structure of E.COLI glpg at pH 4.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NJN
Type: protein
Length: 182 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rhomboid protease glpg
EC: 3.4.21.105
UniProt: P09391
Pockets: 3 · best druggability 0.37

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rhomboid protease glpg (EC 3.4.21.105)	protein	182	76% helix, 0% strand	P09391

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	56	0.37	0.78	11	empty
2	58	0.33	0.76	15	empty
3	64	0.32	0.75	15	empty

Compared structures

4NJN · Crystal Structure of E.coli GlpG at pH 4.5 · 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 4NJN · PDBe 4NJN · UniProt P09391

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