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Crystal structure of ubiquitin conjugating enzyme E2 from plasmodium falciparum

Analyse Crystal structure of ubiquitin conjugating enzyme E2 from plasmodium falciparum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2H2Y
Type
protein
Length
471 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin-conjugating enzyme
EC
6.3.2.19
UniProt
Q8IDP1
Pockets
6 · best druggability 0.81

Structure

x-ray diffraction · 3 distinct chains · 23% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitin-conjugating enzyme (EC 6.3.2.19)protein13322% helix, 19% strandQ8IDP1
B, CUbiquitin-conjugating enzyme (EC 6.3.2.19)protein11325% helix, 21% strandQ8IDP1
DUbiquitin-conjugating enzyme (EC 6.3.2.19)protein11224% helix, 23% strandQ8IDP1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110020.810.8391empty
21490.520.8028empty
31280.500.8024empty
41300.460.7717empty
5660.400.8015empty

Interfaces

5 interfaces between chains.

  • C–D · 680 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 620 Ų buried · 8 hydrogen bonds · protein-protein
  • B–D · 303 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 291 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 46 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 2H2Y · Crystal structure of ubiquitin conjugating enzyme E2 from plasmodium falciparum · the same entry in another collection · chain A against A, TM-score 1.00

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