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Mm-cpn wildtype with ATP

Analyse Mm-cpn wildtype with ATP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3IZM
Type
protein
Length
8,208 residues
Chains
16
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperonin
UniProt
Q877G8
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 53% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, PChaperoninprotein51353% helix, 18% strandQ877G8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15380.840.9070empty
25400.840.9068empty
35380.840.9069empty
45850.840.8973empty
55340.840.9070empty

Interfaces

28 interfaces between chains.

  • I–J · 2102 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 2102 Ų buried · 19 hydrogen bonds · protein-protein
  • I–P · 2101 Ų buried · 19 hydrogen bonds · protein-protein
  • O–P · 2101 Ų buried · 19 hydrogen bonds · protein-protein
  • F–G · 2100 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 3IZM · Mm-cpn wildtype with ATP · the same entry in another collection · chain A against A, TM-score 1.00

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