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Crystal structure of the cytosolic domain of human MID51

Analyse Crystal structure of the cytosolic domain of human MID51 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NXT
Type
protein
Length
1,325 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mitochondrial dynamic protein MID51
UniProt
Q9NQG6
Ligands
SO4
Pockets
10 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 49% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMitochondrial dynamic protein MID51protein33748% helix, 18% strandQ9NQG6
B, CMitochondrial dynamic protein MID51protein33148% helix, 18% strandQ9NQG6
DMitochondrial dynamic protein MID51protein32650% helix, 17% strandQ9NQG6

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A, C
  • GOL · Glycerol · additive · 10 copies · chains A, B, C, D

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

Pockets

10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17820.820.8584empty
24870.790.8651GOL
37370.740.7974empty
46240.740.8087empty
56690.730.7972GOL

Interfaces

2 interfaces between chains.

  • A–B · 636 Ų buried · 4 hydrogen bonds · protein-protein
  • C–D · 580 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 4NXT · Crystal structure of the cytosolic domain of human MiD51 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NQG6 · AlphaFold monomer V2.0 prediction for mitochondrial dynamics protein MID51 (Q9NQG6) · a predicted model of the same protein · chain D against A, TM-score 0.98

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