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Crystal structure of the cytosolic domain of mouse MID51 H201A mutant

Analyse Crystal structure of the cytosolic domain of mouse MID51 H201A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OAH
Type: protein
Length: 1,314 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitochondrial dynamic protein MID51
UniProt: Q8BGV8
Ligands: SO4
Pockets: 11 · best druggability 0.76

Structure

x-ray diffraction · 3 distinct chains · 47% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D	Mitochondrial dynamic protein MID51	protein	330	47% helix, 18% strand	Q8BGV8
B	Mitochondrial dynamic protein MID51	protein	327	48% helix, 18% strand	Q8BGV8
C	Mitochondrial dynamic protein MID51	protein	327	47% helix, 18% strand	Q8BGV8

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, D, C, B

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

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	957	0.76	0.79	109	SO4
2	807	0.73	0.78	96	SO4
3	735	0.73	0.79	85	SO4
4	771	0.73	0.78	91	SO4
5	131	0.56	0.83	30	empty

Interfaces

3 interfaces between chains.

A–C · 1205 Å² buried · 17 hydrogen bonds · protein-protein
B–D · 1079 Å² buried · 15 hydrogen bonds · protein-protein
A–D · 424 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

4OAH · Crystal structure of the cytosolic domain of mouse MiD51 H201A mutant · the same entry in another collection · chain A against A, TM-score 1.00
Q8BGV8 · AlphaFold monomer V2.0 prediction for mitochondrial dynamics protein MID51 (Q8BGV8) · a predicted model of the same protein · chain C against A, TM-score 0.98

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 4OAH · PDBe 4OAH · UniProt Q8BGV8

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