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Cryo-EM structure of the anaphase-promoting COMPLEX/CYCLOSOME, in complex with the NEK2A substrate at 3.9 ångström resolution

Analyse Cryo-EM structure of the anaphase-promoting COMPLEX/CYCLOSOME, in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6TM5
Type
protein
Length
8,117 residues
Chains
22
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Anaphase-promoting complex subunit 1; Anaphase-promoting complex subunit 11; Cell…
EC
2.7.11.1
UniProt
Q9H1A4, Q9NYG5, Q9UJX2, P60006, Q96DE5, P30260, Q8NHZ8, Q9UJX5, Q13042, Q9UM13, Q9BS18, Q9UJX6, Q9UJX4, Q9UJX3, P51955
Ligands
ZN
Pockets
20 · best druggability 0.87

Structure

electron microscopy · 22 distinct chains · 60% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAnaphase-promoting complex subunit 1protein156939% helix, 12% strandQ9H1A4
BAnaphase-promoting complex subunit 11protein8417% helix, 18% strandQ9NYG5
CCell division cycle protein 23 homologprotein52473% helix, 0% strandQ9UJX2
DAnaphase-promoting complex subunit 15protein5535% helix, 0% strandP60006
EAnaphase-promoting complex subunit 16protein5682% helix, 0% strandQ96DE5
FCell division cycle protein 27 homologprotein46073% helix, 0% strandP30260
GAnaphase-promoting complex subunit CDC26protein2536% helix, 0% strandQ8NHZ8
HCell division cycle protein 27 homologprotein48876% helix, 0% strandP30260
IAnaphase-promoting complex subunit 4protein73633% helix, 23% strandQ9UJX5
JCell division cycle protein 16 homologprotein50473% helix, 0% strandQ13042
KCell division cycle protein 16 homologprotein49376% helix, 0% strandQ13042
LAnaphase-promoting complex subunit 10protein1829% helix, 29% strandQ9UM13
MAnaphase-promoting complex subunit 13protein5920% helix, 3% strandQ9BS18
NAnaphase-promoting complex subunit 2protein67663% helix, 3% strandQ9UJX6
OAnaphase-promoting complex subunit 5protein68872% helix, 0% strandQ9UJX4
PCell division cycle protein 23 homologprotein49274% helix, 0% strandQ9UJX2
TAPC1 loopprotein150% helix, 0% strand—
WAnaphase-promoting complex subunit CDC26protein2638% helix, 0% strandQ8NHZ8
XAnaphase-promoting complex subunit 7protein48475% helix, 0% strandQ9UJX3
YAnaphase-promoting complex subunit 7protein49676% helix, 0% strandQ9UJX3
SSERINE/THREONINE-protein kinase NEK2 (EC 2.7.11.1)protein20% helix, 0% strandP51955
QSERINE/THREONINE-protein kinase NEK2 (EC 2.7.11.1)protein30% helix, 0% strandP51955

Ligands and binding sites

  • ZN · Zinc ion · metal · 3 copies · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18990.870.8986empty
29850.870.8986empty
310300.860.8796empty
411500.850.86122empty
510620.830.8486empty

Interfaces

51 interfaces between chains.

  • A–O · 5108 Ų buried · 33 hydrogen bonds · protein-protein
  • I–O · 3218 Ų buried · 21 hydrogen bonds · protein-protein
  • F–H · 2824 Ų buried · 28 hydrogen bonds · protein-protein
  • J–K · 2634 Ų buried · 42 hydrogen bonds · protein-protein
  • X–Y · 2480 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 6TM5 · Cryo-EM structure of the Anaphase-promoting complex/Cyclosome, in complex with the Nek2A… · the same entry in another collection · chain K against K, TM-score 1.00

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