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E134A mutant nucleoside diphosphate kinase derived from halomonas sp. 593

Analyse E134A mutant nucleoside diphosphate kinase derived from halomonas sp. 593 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VGU
Type
protein
Length
1,118 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleoside diphosphate kinase
EC
2.7.4.6
UniProt
Q83WH5
Pockets
13 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, GNucleoside diphosphate kinase (EC 2.7.4.6)protein14046% helix, 20% strandQ83WH5
HNucleoside diphosphate kinase (EC 2.7.4.6)protein13843% helix, 22% strandQ83WH5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19530.840.8575empty
210820.820.8387empty
31490.790.9625empty
4550.730.9916empty
51650.510.7823empty

Interfaces

16 interfaces between chains.

  • C–G · 888 Ų buried · 22 hydrogen bonds · protein-protein
  • D–H · 879 Ų buried · 24 hydrogen bonds · protein-protein
  • A–E · 873 Ų buried · 18 hydrogen bonds · protein-protein
  • B–F · 866 Ų buried · 21 hydrogen bonds · protein-protein
  • B–C · 553 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 3VGU · E134A mutant nucleoside diphosphate kinase derived from Halomonas sp. 593 · the same entry in another collection · chain A against A, TM-score 1.00

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