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Human RAVER1 RRM1 domain in complex with human vinculin tail domain vt

Analyse Human RAVER1 RRM1 domain in complex with human vinculin tail domain vt in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3H2V
Type
protein
Length
977 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Vinculin; Raver-1
UniProt
B4DTM7, Q8IY67
Pockets
8 · best druggability 0.79

Structure

x-ray diffraction · 6 distinct chains · 64% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVinculinprotein17471% helix, 2% strandB4DTM7
BVinculinprotein16774% helix, 1% strandB4DTM7
CVinculinprotein16774% helix, 1% strandB4DTM7
DVinculinprotein17571% helix, 2% strandB4DTM7
E, GRaver-1protein7424% helix, 31% strandQ8IY67
F, HRaver-1protein7325% helix, 36% strandQ8IY67

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17910.790.8285empty
27400.740.8060empty
31640.450.7523empty
41670.450.7524empty
5920.350.7519empty

Interfaces

10 interfaces between chains.

  • B–F · 685 Ų buried · 14 hydrogen bonds · protein-protein
  • C–G · 676 Ų buried · 13 hydrogen bonds · protein-protein
  • D–H · 663 Ų buried · 9 hydrogen bonds · protein-protein
  • A–E · 660 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 377 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 3H2V · Human raver1 RRM1 domain in complex with human vinculin tail domain Vt · the same entry in another collection · chain H against H, TM-score 1.00
  • Q8IY67 · AlphaFold monomer V2.0 prediction for ribonucleoprotein ptb-binding 1 (Q8IY67) · a predicted model of the same protein · chain F against A, TM-score 0.99

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