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2.45A resolution structure of apo independent phosphoglycerate mutase from C. elegans (orthorhombic form)

Analyse 2.45A resolution structure of apo independent phosphoglycerate mutase from C.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5KGL
Type
protein
Length
1,040 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
EC
5.4.2.12
UniProt
G5EFZ1
Ligands
MN, ZN, SO4, CL
Pockets
5 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B2,3-bisphosphoglycerate-independent phosphoglycerate mutase (EC 5.4.2.12)protein52037% helix, 16% strandG5EFZ1

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 2 copies · chains A, B
  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 7 copies · chains A, B
  • CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13980.690.8143empty
210900.690.7481empty
31010.470.8016empty
4810.410.7813empty
5930.320.7220empty

Interfaces

1 interface between chains.

  • A–B · 601 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 5KGL · 2.45A resolution structure of Apo independent phosphoglycerate mutase from C. elegans… · the same entry in another collection · chain A against A, TM-score 1.00
  • G5EFZ1 · AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- independent… · a predicted model of the same protein · chain A against A, TM-score 0.90

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