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Crystal structure of the cytosolic domain of mouse MID51 dimer mutant

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

PDB: 4OAI
Type: protein
Length: 328 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitochondrial dynamic protein MID51
UniProt: Q8BGV8
Ligands: SO4
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
Z	Mitochondrial dynamic protein MID51	protein	328	48% helix, 19% strand	Q8BGV8

Ligands and binding sites

SO4 · Sulfate ion · ion · chains Z

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	768	0.73	0.79	62	SO4
2	71	0.35	0.76	18	empty

Compared structures

4OAI · Crystal structure of the cytosolic domain of mouse MiD51 dimer mutant · the same entry in another collection · chain Z against Z, TM-score 1.00
Q8BGV8 · AlphaFold monomer V2.0 prediction for mitochondrial dynamics protein MID51 (Q8BGV8) · a predicted model of the same protein · chain Z against A, TM-score 0.95

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 Q8BGV8
Elsewhere: RCSB PDB 4OAI · PDBe 4OAI · UniProt Q8BGV8

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