Research workbench

ADP-bound human mitochondrial HSP60-HSP10 football complex

Analyse ADP-bound human mitochondrial HSP60-HSP10 football complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6MRC
Type: protein
Length: 8,792 residues
Chains: 28
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 60 kda heat shock protein, mitochondrial; 10 kda heat shock protein, mitochondrial
EC: 3.6.4.9
UniProt: P10809, P61604
Ligands: ADP, MG
Pockets: 20 · best druggability 0.83

Structure

electron microscopy · 2 distinct chains · 41% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
H, N, M, L, K, J, I, D, C, B, A, G, F, E	60 kda heat shock protein, mitochondrial (EC 3.6.4.9)	protein	528	48% helix, 16% strand	P10809
V, 2, 1, Z, Y, X, W, R, Q, P, O, U, T, S	10 kda heat shock protein, mitochondrial	protein	100	3% helix, 38% strand	P61604

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 14 copies · chains H, N, M, L, K, J, I, D, C, B, A, G, F, E
MG · Magnesium ion · metal · 14 copies · chains H, N, M, L, K, J, I, D, C, B, A, G, F, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	880	0.83	0.85	83	ADP, MG
2	889	0.83	0.85	82	ADP, MG
3	513	0.82	0.88	57	ADP, MG
4	527	0.82	0.88	60	ADP, MG
5	553	0.82	0.87	61	ADP, MG

Interfaces

70 interfaces between chains.

M–L · 1948 Å² buried · 20 hydrogen bonds · protein-protein
G–F · 1932 Å² buried · 20 hydrogen bonds · protein-protein
J–I · 1930 Å² buried · 20 hydrogen bonds · protein-protein
H–N · 1924 Å² buried · 20 hydrogen bonds · protein-protein
C–B · 1921 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

6MRC · ADP-bound human mitochondrial Hsp60-Hsp10 football complex · the same entry in another collection · chain Q against Q, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P10809
Every structure of UniProt P61604
Elsewhere: RCSB PDB 6MRC · PDBe 6MRC · UniProt P10809 · UniProt P61604

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