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Dolichyl phosphate mannose synthase in complex with GDP and dolichyl phosphate mannose

Analyse Dolichyl phosphate mannose synthase in complex with GDP and dolichyl phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5MM1
Type: protein
Length: 346 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dolichol monophosphate mannose synthase
UniProt: Q8U4M3
Ligands: GDP, MJC
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dolichol monophosphate mannose synthase	protein	346	55% helix, 12% strand	Q8U4M3

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MJC · dolichyl phosphate mannose · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	390	0.65	0.79	48	GDP
2	197	0.52	0.77	23	empty
3	87	0.39	0.76	19	empty

Compared structures

5MM1 · Dolichyl phosphate mannose synthase in complex with GDP and dolichyl phosphate mannose · the same entry in another collection · chain A against A, TM-score 1.00

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 Q8U4M3
Elsewhere: RCSB PDB 5MM1 · PDBe 5MM1 · UniProt Q8U4M3

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