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Crystal structure of MMM1

Analyse Crystal structure of MMM1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5YK6
Type: protein
Length: 239 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Maintenance of mitochondrial morphology protein 1
UniProt: C5DRQ1
Ligands: 3PH
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Maintenance of mitochondrial morphology protein 1	protein	239	28% helix, 33% strand	C5DRQ1

Ligands and binding sites

3PH · 1,2-diacyl-glycerol-3-sn-phosphate · ligand · 2 copies · chains A

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

Pockets

4 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	911	0.76	0.79	65	empty
2	57	0.43	0.82	13	empty
3	98	0.36	0.74	16	empty
4	70	0.31	0.74	14	empty

Compared structures

5YK6 · Crystal Structure of Mmm1 · the same entry in another collection · chain A against A, TM-score 1.00
C5DRQ1 · AlphaFold monomer V2.0 prediction for maintenance of mitochondrial morphology protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 C5DRQ1
Elsewhere: RCSB PDB 5YK6 · PDBe 5YK6 · UniProt C5DRQ1

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