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Structure of the intracellular kinase homology domain of RV3910 at 2.2 a resolution

Analyse Structure of the intracellular kinase homology domain of RV3910 at 2.2 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3UQC
Type
protein
Length
989 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Probable conserved transmembrane protein
UniProt
O05435
Pockets
11 · best druggability 0.69

Structure

x-ray diffraction · 4 distinct chains · 36% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProbable conserved transmembrane proteinprotein24635% helix, 23% strandO05435
BProbable conserved transmembrane proteinprotein24436% helix, 22% strandO05435
CProbable conserved transmembrane proteinprotein25036% helix, 22% strandO05435
DProbable conserved transmembrane proteinprotein24936% helix, 21% strandO05435

Ligands and binding sites

  • SIN · Succinic acid · additive · chains B

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

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16420.690.7748empty
25390.660.7747empty
32450.520.7631empty
41170.430.7727empty
51130.420.7727empty

Interfaces

4 interfaces between chains.

  • B–C · 641 Ų buried · 11 hydrogen bonds · protein-protein
  • A–D · 602 Ų buried · 15 hydrogen bonds · protein-protein
  • C–D · 201 Ų buried · 2 hydrogen bonds · protein-protein
  • A–C · 60 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 3UQC · Structure of the Intracellular Kinase Homology Domain of Rv3910 at 2.2 A resolution · the same entry in another collection · chain A against A, TM-score 1.00

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