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Atomic model of mm-cpn in the closed state

Analyse Atomic model of mm-cpn in the closed state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3LOS
Type
protein
Length
8,512 residues
Chains
16
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperonin
UniProt
Q877G8
Pockets
20 · best druggability 0.89

Structure

electron microscopy · 1 distinct chain · 38% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, PChaperoninprotein53238% helix, 2% strandQ877G8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16980.890.93111empty
26510.880.93120empty
39130.880.90136empty
49030.880.90141empty
510100.870.88138empty

Interfaces

56 interfaces between chains.

  • G–H · 3013 Ų buried · 42 hydrogen bonds · protein-protein
  • K–L · 3012 Ų buried · 42 hydrogen bonds · protein-protein
  • M–N · 3012 Ų buried · 42 hydrogen bonds · protein-protein
  • A–B · 3011 Ų buried · 42 hydrogen bonds · protein-protein
  • A–H · 3007 Ų buried · 43 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 disulfide (disulfide).

Compared structures

  • 3LOS · Atomic Model of Mm-cpn in the Closed State · the same entry in another collection · chain C against C, TM-score 1.00

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