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Crystal structure of the E. COLI glycerol facilitator (glpf) mutation W48F, F200T

Analyse Crystal structure of the E. COLI glycerol facilitator (glpf) mutation W48F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LDF
Type: protein
Length: 254 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycerol uptake facilitator protein
UniProt: P11244
Ligands: MG
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycerol uptake facilitator protein	protein	254	75% helix, 0% strand	P11244

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A
BOG · octyl beta-D-glucopyranoside · additive · 2 copies · chains A
GOL · Glycerol · additive · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	395	0.72	0.83	52	GOL

Compared structures

1LDF · Crystal structure of the E. COLI glycerol facilitator (glpf) mutation W48F, F200T · 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 P11244
Elsewhere: RCSB PDB 1LDF · PDBe 1LDF · UniProt P11244

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