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Crystal structure of ef-TU/CDIA/CDII

Analyse Crystal structure of ef-TU/CDIA/CDII in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7VMC
Type
protein
Length
672 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Elongation factor tu; TRNA nuclease cdia; Contact-dependent inhibitor I
EC
3.1.-.-
UniProt
E2QJ06, B3BM48, A0A2A3ULE6
Pockets
11 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 21% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AElongation factor tuprotein38421% helix, 35% strandE2QJ06
BTRNA nuclease cdia (EC 3.1.-.-)protein11134% helix, 26% strandB3BM48
CContact-dependent inhibitor Iprotein17710% helix, 38% strandA0A2A3ULE6

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1860.760.9726empty
26360.670.7760empty
32670.630.8140empty
41020.630.8723empty
52820.560.7734empty

Interfaces

3 interfaces between chains.

  • B–C · 1247 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 995 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 21 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7VMC · Crystal structure of EF-Tu/CdiA/CdiI · the same entry in another collection · chain A against A, TM-score 1.00

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