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Human mitochondrial chaperonin MHSP60

Analyse Human mitochondrial chaperonin MHSP60 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7L7S
Type
protein
Length
3,668 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
60 kda heat shock protein, mitochondrial
EC
5.6.1.7
UniProt
P10809
Pockets
20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 47% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
H, I, J, K, L, M, N60 kda heat shock protein, mitochondrial (EC 5.6.1.7)protein52447% helix, 11% strandP10809

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11340.780.9639empty
28440.780.81119empty
31310.780.9640empty
41290.770.9538empty
51300.770.9540empty

Interfaces

7 interfaces between chains.

  • I–J · 1347 Ų buried · 14 hydrogen bonds · protein-protein
  • H–N · 1346 Ų buried · 15 hydrogen bonds · protein-protein
  • K–L · 1343 Ų buried · 14 hydrogen bonds · protein-protein
  • H–I · 1342 Ų buried · 14 hydrogen bonds · protein-protein
  • J–K · 1341 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 7L7S · Human mitochondrial chaperonin mHsp60 · the same entry in another collection · chain N against N, TM-score 1.00
  • P10809 · AlphaFold monomer V2.0 prediction for 60 kda heat shock protein, mitochondrial (P10809) · a predicted model of the same protein · chain K against A, TM-score 0.66

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