Research workbench

HTLV-1 GP21 ECTODOMAIN/MALTOSE-binding protein chimera

Analyse HTLV-1 GP21 ECTODOMAIN/MALTOSE-binding protein chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MG1
Type: protein
Length: 450 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (HTLV-1 GP21 ECTODOMAIN/MALTOSE-binding protein chimera)
UniProt: P02928
Ligands: GLC, CL
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (HTLV-1 GP21 ECTODOMAIN/MALTOSE-binding protein chimera)	protein	450	49% helix, 17% strand	P02928

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
CL · Chloride 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	370	0.70	0.82	31	GLC
2	81	0.39	0.77	22	empty
3	66	0.30	0.74	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1MG1 · HTLV-1 GP21 ECTODOMAIN/MALTOSE-binding protein chimera · 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 P02928
Elsewhere: RCSB PDB 1MG1 · PDBe 1MG1 · UniProt P02928

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.