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Human M2 pyruvate kinase

Analyse Human M2 pyruvate kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3SRH
Type
protein
Length
2,072 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Pyruvate kinase isozymes M1/M2
EC
2.7.1.40
UniProt
P14618
Ligands
PO4
Pockets
20 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DPyruvate kinase isozymes M1/M2 (EC 2.7.1.40)protein51838% helix, 20% strandP14618

Ligands and binding sites

  • PO4 · Phosphate ion · ion · 3 copies · chains A, B, D

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

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18250.860.8955empty
22860.860.9641empty
33270.860.9543empty
42760.740.8732empty
55900.720.8077empty

Interfaces

6 interfaces between chains.

  • B–C · 2819 Ų buried · 39 hydrogen bonds · protein-protein
  • A–D · 2815 Ų buried · 33 hydrogen bonds · protein-protein
  • C–D · 1475 Ų buried · 19 hydrogen bonds · protein-protein
  • A–B · 1418 Ų buried · 23 hydrogen bonds · protein-protein
  • B–D · 46 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 3SRH · Human M2 pyruvate kinase · the same entry in another collection · chain A against A, TM-score 1.00

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