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Mannosyl-3-phosphoglycerate synthase from thermus thermophilus HB27 apoprotein

Analyse Mannosyl-3-phosphoglycerate synthase from thermus thermophilus HB27 apoprotein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2WVK
Type
protein
Length
773 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mannosyl-3-phosphoglycerate synthase
EC
2.4.1.217
UniProt
Q72K30
Ligands
ZN
Pockets
8 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMannosyl-3-phosphoglycerate synthase (EC 2.4.1.217)protein39144% helix, 17% strandQ72K30
BMannosyl-3-phosphoglycerate synthase (EC 2.4.1.217)protein38243% helix, 18% strandQ72K30

Ligands and binding sites

  • ZN · Zinc ion · metal · 5 copies · chains A, B
  • FLC · Citrate anion · additive · 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17800.780.8256empty
27410.730.7858empty
33880.620.7730empty
41030.380.7617empty
51020.380.7621FLC

Interfaces

1 interface between chains.

  • A–B · 1749 Ų buried · 38 hydrogen bonds · protein-protein

Compared structures

  • 2WVK · Mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 apoprotein · the same entry in another collection · chain A against A, TM-score 1.00

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