Research workbench
Crystal structure of the human mitochondrial chaperonin symmetrical 'football' complex
Analyse Crystal structure of the human mitochondrial chaperonin symmetrical 'football'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PJ1
- Type
- protein
- Length
- 8,783 residues
- Chains
- 28
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 60 kda heat shock protein, mitochondrial; 10 kda heat shock protein, mitochondrial
- UniProt
- P10809, P61604
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 6 distinct chains · 26% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | 60 kda heat shock protein, mitochondrial | protein | 526 | 51% helix, 18% strand | P10809 |
| O, Q, R, S, T, V, W, X, Y, 1 | 10 kda heat shock protein, mitochondrial | protein | 100 | 0% helix, 40% strand | P61604 |
| P | 10 kda heat shock protein, mitochondrial | protein | 105 | 0% helix, 38% strand | P61604 |
| U | 10 kda heat shock protein, mitochondrial | protein | 102 | 0% helix, 45% strand | P61604 |
| Z | 10 kda heat shock protein, mitochondrial | protein | 108 | 0% helix, 35% strand | P61604 |
| 2 | 10 kda heat shock protein, mitochondrial | protein | 104 | 0% helix, 38% strand | P61604 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 14 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N
- MG · Magnesium ion · metal · 14 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 726 | 0.81 | 0.85 | 70 | ADP, MG |
| 2 | 392 | 0.81 | 0.90 | 54 | ADP, MG |
| 3 | 699 | 0.81 | 0.85 | 69 | ADP, MG |
| 4 | 437 | 0.80 | 0.88 | 61 | ADP, MG |
| 5 | 462 | 0.80 | 0.87 | 56 | ADP, MG |
Interfaces
67 interfaces between chains.
- B–C · 2278 Ų buried · 29 hydrogen bonds · protein-protein
- D–E · 2025 Ų buried · 28 hydrogen bonds · protein-protein
- A–G · 1975 Ų buried · 25 hydrogen bonds · protein-protein
- I–J · 1971 Ų buried · 25 hydrogen bonds · protein-protein
- K–L · 1959 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 4PJ1 · Crystal structure of the human mitochondrial chaperonin symmetrical 'football' complex · the same entry in another collection · chain K against K, 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 4PJ1 · PDBe 4PJ1 · UniProt P10809 · UniProt P61604
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