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Fitted coordinates for groel-ADP7-groes cryo-EM complex (emd-1181)

Analyse Fitted coordinates for groel-ADP7-groes cryo-EM complex (emd-1181) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2C7D
Type
protein
Length
7,966 residues
Chains
21
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
60 kda chaperonin; 10 kda chaperonin molecule: groes, protein CPN10, groes protein
UniProt
P0A6F5, P0A6F9
Pockets
20 · best druggability 0.82

Structure

electron microscopy · 3 distinct chains · 47% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G60 kda chaperoninprotein52451% helix, 18% strandP0A6F5
H, I, J, K, L, M, N60 kda chaperoninprotein52251% helix, 17% strandP0A6F5
O, P, Q, R, S, T, U10 kda chaperonin molecule: groes, protein CPN10, groes proteinprotein923% helix, 36% strandP0A6F9

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15080.820.8973empty
210170.820.83110empty
35080.810.8871empty
410480.810.82110empty
58620.810.83116empty

Interfaces

47 interfaces between chains.

  • C–D · 1844 Ų buried · 24 hydrogen bonds · protein-protein
  • A–B · 1796 Ų buried · 22 hydrogen bonds · protein-protein
  • E–F · 1779 Ų buried · 25 hydrogen bonds · protein-protein
  • F–G · 1761 Ų buried · 27 hydrogen bonds · protein-protein
  • A–G · 1744 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 2C7D · Fitted coordinates for GroEL-ADP7-GroES Cryo-EM complex (EMD-1181) · the same entry in another collection · chain K against K, TM-score 1.00

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