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Pfmcm-aaa double-octamer

Analyse Pfmcm-aaa double-octamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4R7Z
Type
protein
Length
5,056 residues
Chains
16
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cell division control protein 21
UniProt
Q8U3I4
Ligands
ADP, MG
Pockets
20 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, PCell division control protein 21protein31643% helix, 9% strandQ8U3I4

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 16 copies · chains A, H, B, C, D, E, F, G, I, P, J, K, L, M, N, O
  • MG · Magnesium ion · metal · 16 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P

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
17080.850.89100ADP, MG
28060.850.8886ADP, MG
39060.850.8798ADP, MG
48680.840.8799ADP, MG
57730.840.8790ADP, MG

Interfaces

32 interfaces between chains.

  • O–P · 1295 Ų buried · 14 hydrogen bonds · protein-protein
  • A–H · 1252 Ų buried · 14 hydrogen bonds · protein-protein
  • J–K · 1244 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 1231 Ų buried · 17 hydrogen bonds · protein-protein
  • K–L · 1230 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 4R7Z · PfMCM-AAA double-octamer · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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