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Crystal structure of gida from E. COLI

Analyse Crystal structure of gida from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3CP2
Type
protein
Length
491 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRNA uridine 5-carboxymethylaminomethyl modification enzyme gida
EC
1.-.-.-
UniProt
P0A6U3
Ligands
SO4
Pockets
6 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATRNA uridine 5-carboxymethylaminomethyl modification enzyme gida (EC 1.-.-.-)protein49135% helix, 18% strandP0A6U3

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14920.660.7860SO4
22760.590.7832empty
31030.390.7619empty
4510.330.7818empty
5600.330.7715empty

Compared structures

  • 3CP2 · Crystal structure of GidA from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A6U3 · AlphaFold monomer V2.0 prediction for tRNA uridine 5-carboxymethylaminomethyl… · a predicted model of the same protein · chain A against A, TM-score 0.97

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