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Crystal structure of phosphoglycerate kinase from thermus thermophilus HB8

Analyse Crystal structure of phosphoglycerate kinase from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1V6S
Type
protein
Length
780 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosphoglycerate kinase
EC
2.7.2.3
UniProt
P09403
Ligands
NA
Pockets
7 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPhosphoglycerate kinase (EC 2.7.2.3)protein39040% helix, 17% strandP09403

Ligands and binding sites

  • NA · Sodium ion · metal · 3 copies · chains A, B
  • GOL · Glycerol · additive · 4 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12110.590.8134empty
22050.560.7930empty
31110.400.7535empty
4580.390.8023empty
5690.320.7617empty

Compared structures

  • 1V6S · Crystal Structure of Phosphoglycerate Kinase from Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00
  • P09403 · AlphaFold monomer V2.0 prediction for phosphoglycerate kinase (P09403) · a predicted model of the same protein · chain A against A, TM-score 0.98

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