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S8-msrk-S8-SP11 complex

Analyse S8-msrk-S8-SP11 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6KYW
Type
protein
Length
867 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Receptor protein kinase SRK8; S locus protein 11
UniProt
Q39276, Q9SE17
Ligands
NAG
Pockets
12 · best druggability 0.84

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AReceptor protein kinase SRK8protein3897% helix, 43% strandQ39276
BReceptor protein kinase SRK8protein3866% helix, 41% strandQ39276
C, DS locus protein 11protein4615% helix, 35% strandQ9SE17

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B

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

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18550.840.8696empty
27970.830.8698empty
31770.520.7930empty
41980.500.7728empty
51010.480.8016empty

Interfaces

6 interfaces between chains.

  • B–C · 904 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 899 Ų buried · 6 hydrogen bonds · protein-protein
  • A–D · 788 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 469 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 463 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide, 5 glycan (disulfide, N-glycosylation).

Compared structures

  • 6KYW · S8-mSRK-S8-SP11 complex · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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