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Crystal structure of APC11 ring domain

Analyse Crystal structure of APC11 ring domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4R2Y
Type
protein
Length
250 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Anaphase-promoting complex subunit 11
UniProt
Q9NYG5
Ligands
ZN
Pockets
3 · best druggability 0.54

Structure

x-ray diffraction · 4 distinct chains · 19% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAnaphase-promoting complex subunit 11protein6422% helix, 19% strandQ9NYG5
BAnaphase-promoting complex subunit 11protein5919% helix, 20% strandQ9NYG5
CAnaphase-promoting complex subunit 11protein6517% helix, 18% strandQ9NYG5
DAnaphase-promoting complex subunit 11protein6218% helix, 19% strandQ9NYG5

Ligands and binding sites

  • ZN · Zinc ion · metal · 12 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11910.540.7827empty
21140.480.8022empty
3520.250.7212empty

Interfaces

5 interfaces between chains.

  • A–B · 1411 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 1410 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 459 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 23 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 15 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4R2Y · Crystal structure of APC11 RING domain · the same entry in another collection · chain C against C, TM-score 1.00
  • Q9NYG5 · AlphaFold monomer V2.0 prediction for anaphase-promoting complex subunit 11 (Q9NYG5) · a predicted model of the same protein · chain B against A, TM-score 0.69

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