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Structure of the K. lactis CBF3 core - NDC10 D1 complex

Analyse Structure of the K. lactis CBF3 core - NDC10 D1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6P7W
Type
protein
Length
1,542 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NDC10; CTF13; SKP1; CEP3
UniProt
Q6CPM4, Q6CK37, O94228, Q6CRD4
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 5 distinct chains · 59% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ENDC10protein9471% helix, 0% strandQ6CPM4
CCTF13protein38727% helix, 17% strandQ6CK37
DSKP1protein12655% helix, 13% strandO94228
BCEP3protein47671% helix, 0% strandQ6CRD4
ACEP3protein45972% helix, 0% strandQ6CRD4

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15310.840.8968empty
27780.800.8475empty
31440.790.9538empty
44750.760.8450empty
58090.750.8083empty

Interfaces

5 interfaces between chains.

  • B–A · 1482 Ų buried · 10 hydrogen bonds · protein-protein
  • C–B · 1343 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 1066 Ų buried · 4 hydrogen bonds · protein-protein
  • E–C · 822 Ų buried · 7 hydrogen bonds · protein-protein
  • D–B · 315 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6P7W · Structure of the K. lactis CBF3 core - Ndc10 D1 complex · the same entry in another collection · chain E against E, TM-score 1.00

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