MolNFT v1 · #127080 · protein

Dolichyl phosphate mannose synthase in complex with GDP-mannose and MN2+ (donor complex)

5MM0 · Dolichol monophosphate mannose synthase: “Dolichyl phosphate mannose synthase in complex with GDP-mannose and MN2+ (donor complex)”. X-ray diffraction, 3 ligands (GDD, MN, CL), 2 pockets (best druggability 0.78). MolNFT v1 #127080…

PDB: 5MM0
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dolichol monophosphate mannose synthase
UniProt: Q8U4M3
Ligands: GDD, MN, CL
Pockets: 2 · best druggability 0.78

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	355	55% helix, 12% strand	Q8U4M3

Ligands and binding sites

GDD · Guanosine-5'-diphosphate-alpha-D-mannose · ligand · chains A
MN · Manganese (II) ion · metal · chains A
CL · Chloride ion · ion · chains A
LDA · Lauryl dimethylamine-N-oxide · additive · 5 copies · chains A

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

Pockets

2 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	601	0.78	0.83	49	GDD, MN
2	172	0.54	0.79	23	CL, LDA

Compared structures

5MM0 · Dolichyl phosphate mannose synthase in complex with GDP-mannose and Mn2+ (donor complex) · 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 5MM0 · PDBe 5MM0 · UniProt Q8U4M3

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