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Crystal structure of gae domain of GGA2P from saccharomyces cerevisiae

Analyse Crystal structure of gae domain of GGA2P from saccharomyces cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3MNM
Type
protein
Length
334 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ADP-ribosylation factor-binding protein GGA2
UniProt
P38817
Ligands
SO4
Pockets
4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 60% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BADP-ribosylation factor-binding protein GGA2protein1120% helix, 59% strandP38817
CADP-ribosylation factor-binding protein GGA2protein1100% helix, 62% strandP38817

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
  • GOL · Glycerol · additive · 5 copies · chains A, B, C

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.630.9420empty
21230.480.7925GOL
3730.410.7917GOL
4540.390.8122empty

Interfaces

2 interfaces between chains.

  • A–B · 661 Ų buried · 12 hydrogen bonds · protein-protein
  • B–C · 645 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 modified (methylation).

Compared structures

  • 3MNM · Crystal structure of GAE domain of GGA2p from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
  • P38817 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-binding protein GGA2… · a predicted model of the same protein · chain C against A, TM-score 0.98

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