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Structure of mpt-2, a GDP-man-dependent mannosyltransferase from leishmania mexicana

Analyse Structure of mpt-2, a GDP-man-dependent mannosyltransferase from leishmania… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Q4X
Type
protein
Length
627 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized protein
UniProt
E9AND8
Ligands
NA
Pockets
8 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 9% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUncharacterized proteinprotein3179% helix, 50% strandE9AND8
BUncharacterized proteinprotein3109% helix, 52% strandE9AND8

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11410.730.9231empty
21320.720.9230empty
33440.610.7839empty
42380.520.7628empty
51420.490.7827empty

Interfaces

1 interface between chains.

  • A–B · 1354 Ų buried · 41 hydrogen bonds · protein-protein

Compared structures

  • 6Q4X · Structure of MPT-2, a GDP-Man-dependent mannosyltransferase from Leishmania mexicana · the same entry in another collection · chain A against A, TM-score 1.00

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