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Complex structure of RTT107P and phosphorylated histone H2A

Analyse Complex structure of RTT107P and phosphorylated histone H2A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3T7K
Type
protein
Length
477 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Regulator of TY1 transposition protein 107; Histone H2A.1
UniProt
P38850, P04911
Pockets
5 · best druggability 0.64

Structure

x-ray diffraction · 3 distinct chains · 34% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARegulator of TY1 transposition protein 107protein23334% helix, 17% strandP38850
C, DHistone H2A.1protein50% helix, 20% strandP04911
BRegulator of TY1 transposition protein 107protein23434% helix, 17% strandP38850

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14950.640.7743empty
2660.450.8313empty
3580.420.8213empty
4670.380.7919empty
5540.270.7412empty

Interfaces

3 interfaces between chains.

  • A–B · 465 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 389 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 373 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

  • 3T7K · Complex structure of Rtt107p and phosphorylated histone H2A · the same entry in another collection · chain A against A, TM-score 1.00
  • P38850 · AlphaFold monomer V2.0 prediction for regulator of TY1 transposition protein 107 (P38850) · a predicted model of the same protein · chain B against A, TM-score 0.99
  • P04911 · AlphaFold monomer V2.0 prediction for histone H2A.1 (P04911) · a predicted model of the same protein · chain C against A, TM-score 0.69

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