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X-ray structure of the N-terminal fha domain from S. cerevisiae RAD53P in complex with a phosphothreonine peptide at 1.6 a resolution

Analyse X-ray structure of the N-terminal fha domain from S. cerevisiae RAD53P in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1G6G
Type
protein
Length
271 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein kinase RAD53; Ser-leu-glu-val-tpo-glu-ala-aspala-thr-phe-ala- lys
EC
2.7.1.-
UniProt
P22216
Pockets
2 · best druggability 0.44

Structure

x-ray diffraction · 4 distinct chains · 11% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein kinase RAD53 (EC 2.7.1.-)protein12712% helix, 38% strandP22216
BProtein kinase RAD53 (EC 2.7.1.-)protein12411% helix, 38% strandP22216
ESer-leu-glu-val-tpo-glu-ala-aspala-thr-phe-ala- lysprotein80% helix, 0% strand—
FSer-leu-glu-val-tpo-glu-ala-aspala-thr-phe-ala- lysprotein120% helix, 0% strand—

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11500.440.7621empty
2850.320.7318empty

Interfaces

3 interfaces between chains.

  • B–F · 494 Ų buried · 14 hydrogen bonds · protein-protein
  • A–E · 473 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 288 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 modified (phosphorylation).

Compared structures

  • 1G6G · X-ray structure of the N-terminal fha domain from S. cerevisiae RAD53P in complex with a… · the same entry in another collection · chain A against A, TM-score 1.00
  • P22216 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase RAD53 (P22216) · a predicted model of the same protein · chain B against A, TM-score 0.99

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