Research workbench
Crystal structure of human mitochondrial trifunctional protein
Analyse Crystal structure of human mitochondrial trifunctional protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DV2
- Type
- protein
- Length
- 6,850 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trifunctional enzyme subunit beta, mitochondrial; Trifunctional enzyme subunit alpha…
- EC
- 2.3.1.16, 4.2.1.17, 1.1.1.211
- UniProt
- P55084, P40939
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 8 distinct chains · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trifunctional enzyme subunit beta, mitochondrial (EC 2.3.1.16) | protein | 432 | 33% helix, 19% strand | P55084 |
| B | Trifunctional enzyme subunit beta, mitochondrial (EC 2.3.1.16) | protein | 419 | 34% helix, 19% strand | P55084 |
| C | Trifunctional enzyme subunit beta, mitochondrial (EC 2.3.1.16) | protein | 421 | 33% helix, 19% strand | P55084 |
| D | Trifunctional enzyme subunit beta, mitochondrial (EC 2.3.1.16) | protein | 424 | 34% helix, 19% strand | P55084 |
| E | Trifunctional enzyme subunit beta, mitochondrial (EC 2.3.1.16) | protein | 423 | 34% helix, 19% strand | P55084 |
| F | Trifunctional enzyme subunit beta, mitochondrial (EC 2.3.1.16) | protein | 425 | 35% helix, 19% strand | P55084 |
| G, H | Trifunctional enzyme subunit alpha, mitochondrial (EC 4.2.1.17, 1.1.1.211) | protein | 725 | 50% helix, 11% strand | P40939 |
| I, J, K, L | Trifunctional enzyme subunit alpha, mitochondrial (EC 4.2.1.17, 1.1.1.211) | protein | 714 | 50% helix, 11% strand | P40939 |
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 | 872 | 0.81 | 0.83 | 87 | empty |
| 2 | 874 | 0.80 | 0.83 | 92 | empty |
| 3 | 798 | 0.80 | 0.83 | 86 | empty |
| 4 | 727 | 0.80 | 0.84 | 81 | empty |
| 5 | 951 | 0.80 | 0.81 | 98 | empty |
Interfaces
25 interfaces between chains.
- A–B · 2490 Ų buried · 45 hydrogen bonds · protein-protein
- C–D · 2019 Ų buried · 42 hydrogen bonds · protein-protein
- E–F · 1966 Ų buried · 41 hydrogen bonds · protein-protein
- B–H · 875 Ų buried · 6 hydrogen bonds · protein-protein
- F–L · 863 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 6DV2 · Crystal Structure of Human Mitochondrial Trifunctional Protein · 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 P55084
- Every structure of UniProt P40939
- Elsewhere: RCSB PDB 6DV2 · PDBe 6DV2 · UniProt P55084 · UniProt P40939
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