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X-ray structure of the mannosyltransferase KTR4P from S. cerevisiae in complex with GDP

Analyse X-ray structure of the mannosyltransferase KTR4P from S. cerevisiae in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5A07
Type
protein
Length
789 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Probable mannosyltransferase KTR4
EC
2.4.1.-
UniProt
P38131
Ligands
GDP, MN
Pockets
5 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProbable mannosyltransferase KTR4 (EC 2.4.1.-)protein39546% helix, 12% strandP38131
BProbable mannosyltransferase KTR4 (EC 2.4.1.-)protein39445% helix, 12% strandP38131

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
  • MN · Manganese (II) ion · metal · 2 copies · chains A, B
  • ACT · Acetate ion · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16890.780.8375empty
24740.680.7943GDP, MN
34490.660.7943GDP, MN
4800.460.8119empty
5570.390.8015empty

Interfaces

1 interface between chains.

  • A–B · 830 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 5A07 · X-ray structure of the mannosyltransferase Ktr4p from S. cerevisiae in complex with GDP · the same entry in another collection · chain A against A, TM-score 1.00
  • P38131 · AlphaFold monomer V2.0 prediction for probable mannosyltransferase KTR4 (P38131) · a predicted model of the same protein · chain A against A, TM-score 1.00

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