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Crystal structure of B. subtilis 168 glpq in complex with bicine

Analyse Crystal structure of B. subtilis 168 glpq in complex with bicine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T91
Type: protein
Length: 258 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycerophosphoryl diester phosphodiesterase
EC: 3.1.4.46
UniProt: P37965
Ligands: BCN, CA, NA
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycerophosphoryl diester phosphodiesterase (EC 3.1.4.46)	protein	258	40% helix, 17% strand	P37965

Ligands and binding sites

BCN · Bicine · ligand · chains A
CA · Calcium ion · metal · chains A
NA · Sodium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.37	0.79	13	CA, BCN

Compared structures

5T91 · Crystal structure of B. subtilis 168 GlpQ in complex with bicine · the same entry in another collection · chain A against A, TM-score 1.00
P37965 · AlphaFold monomer V2.0 prediction for glycerophosphodiester phosphodiesterase (P37965) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P37965
Elsewhere: RCSB PDB 5T91 · PDBe 5T91 · UniProt P37965

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