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Crystal structure of saccharomyces cerevisiae MNN9 in complex with GDP and mn.

Analyse Crystal structure of saccharomyces cerevisiae MNN9 in complex with GDP and mn. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZF8
Type: protein
Length: 288 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mannan polymerase complexes subunit MNN9
UniProt: P39107
Ligands: GDP, MN
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mannan polymerase complexes subunit MNN9	protein	288	31% helix, 25% strand	P39107

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MN · Manganese (II) ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	269	0.56	0.77	31	GDP, MN

Compared structures

3ZF8 · Crystal structure of Saccharomyces cerevisiae Mnn9 in complex with GDP and Mn. · the same entry in another collection · chain A against A, TM-score 1.00
P39107 · AlphaFold monomer V2.0 prediction for mannan polymerase complexes subunit MNN9 (P39107) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P39107
Elsewhere: RCSB PDB 3ZF8 · PDBe 3ZF8 · UniProt P39107

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