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MolNFT v1 · #142060 · protein

Structure of human mitochondrial trifunctional protein, octamer

5ZRV · Trifunctional enzyme subunit alpha, mitochondrial: “Structure of human mitochondrial trifunctional protein, octamer”. Electron microscopy, 20 pockets (best druggability 0.78). MolNFT v1 #142060 on GenesisL1: 3D structure, binding…

PDB
5ZRV
Type
protein
Length
4,524 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trifunctional enzyme subunit alpha, mitochondrial; Trifunctional enzyme subunit beta…
EC
4.2.1.17, 1.1.1.211, 2.3.1.16
UniProt
P40939, P55084
Pockets
20 · best druggability 0.78

Structure

electron microscopy · 2 distinct chains · 35% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, GTrifunctional enzyme subunit alpha, mitochondrial (EC 4.2.1.17, 1.1.1.211)protein71140% helix, 9% strandP40939
B, D, F, HTrifunctional enzyme subunit beta, mitochondrial (EC 2.3.1.16)protein42026% helix, 14% strandP55084

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17400.780.83128empty
24100.720.8475empty
38810.710.7795empty
49720.710.76139empty
55370.700.8082empty

Interfaces

12 interfaces between chains.

  • B–D · 495 Ų buried · 4 hydrogen bonds · protein-protein
  • F–H · 495 Ų buried · 4 hydrogen bonds · protein-protein
  • G–H · 96 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 95 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 92 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5ZRV · Structure of human mitochondrial trifunctional protein, octamer · the same entry in another collection · chain H against H, TM-score 1.00
  • P55084 · AlphaFold monomer V2.0 prediction for trifunctional enzyme subunit beta, mitochondrial… · a predicted model of the same protein · chain F against A, TM-score 0.97

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