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Structure of udp-galactopyranose mutase bound to udp-galactose (reduced)

Analyse Structure of udp-galactopyranose mutase bound to udp-galactose (reduced) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3INT
Type
protein
Length
757 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Probable udp-galactopyranose mutase
EC
5.4.99.9
UniProt
Q48485
Ligands
FDA, UDP, GDU
Pockets
5 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProbable udp-galactopyranose mutase (EC 5.4.99.9)protein38334% helix, 21% strandQ48485
BProbable udp-galactopyranose mutase (EC 5.4.99.9)protein37434% helix, 21% strandQ48485

Ligands and binding sites

  • FDA · Dihydroflavine-adenine dinucleotide · ligand · 2 copies · chains A, B
  • UDP · Uridine-5'-diphosphate · ligand · chains A
  • GDU · Galactose-uridine-5'-diphosphate · ligand · chains 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, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17720.850.8881FDA, GDU
210860.850.85102FDA, UDP
310250.760.7969empty
42490.690.8436empty
5510.360.8015empty

Interfaces

1 interface between chains.

  • A–B · 1085 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 3INT · Structure of UDP-galactopyranose mutase bound to UDP-galactose (reduced) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q48485 · AlphaFold monomer V2.0 prediction for udp-galactopyranose mutase (Q48485) · a predicted model of the same protein · chain A against A, TM-score 0.99

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