Research workbench

G51S mutant of L. casei fpgs

Analyse G51S mutant of L. casei fpgs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2GC5
Type: protein
Length: 408 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Folylpolyglutamate synthase
EC: 6.3.2.17
UniProt: P15925
Ligands: SO4
Pockets: 3 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Folylpolyglutamate synthase (EC 6.3.2.17)	protein	408	43% helix, 18% strand	P15925

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	542	0.67	0.78	71	SO4
2	111	0.61	0.86	18	empty
3	54	0.33	0.77	19	empty

Modifications

Observed in the structure: 1 modified (carboxylation).

Compared structures

2GC5 · G51S mutant of L. casei FPGS · the same entry in another collection · chain A against A, TM-score 1.00
P15925 · AlphaFold monomer V2.0 prediction for folylpolyglutamate synthase (P15925) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P15925
Elsewhere: RCSB PDB 2GC5 · PDBe 2GC5 · UniProt P15925

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