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Cryo-EM structure of 9-fold symmetric ratcpn-alpha in apo state

Analyse Cryo-EM structure of 9-fold symmetric ratcpn-alpha in apo state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3J1C
Type
protein
Length
9,342 residues
Chains
18
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chaperonin alpha subunit
UniProt
Q877H0
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 49% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, RChaperonin alpha subunitprotein51949% helix, 16% strandQ877H0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15730.840.8967empty
28160.830.8591empty
34260.830.9057empty
49140.820.84100empty
54980.820.8957empty

Interfaces

27 interfaces between chains.

  • K–L · 1210 Ų buried · 10 hydrogen bonds · protein-protein
  • H–I · 1206 Ų buried · 10 hydrogen bonds · protein-protein
  • F–G · 1128 Ų buried · 11 hydrogen bonds · protein-protein
  • A–I · 1125 Ų buried · 14 hydrogen bonds · protein-protein
  • B–C · 1120 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 3J1C · Cryo-EM structure of 9-fold symmetric rATcpn-alpha in apo state · the same entry in another collection · chain D against D, TM-score 1.00

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