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Complex structure of lf-transferase and peptide B

Analyse Complex structure of lf-transferase and peptide B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Z3N
Type
protein
Length
470 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
LEUCYL/PHENYLALANYL-tRNA-protein transferase; Peptide (PHE)(ARG)(TYR)(LEU)(GLY)
EC
2.3.2.6
UniProt
P0A8P1
Pockets
2 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BLEUCYL/PHENYLALANYL-tRNA-protein transferase (EC 2.3.2.6)protein23034% helix, 26% strandP0A8P1
C, DPeptide (PHE)(ARG)(TYR)(LEU)(GLY)protein560% helix, 0% strand—

Ligands and binding sites

  • TAR · D(-)-tartaric acid · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15700.790.8555empty
2530.280.7517TAR

Interfaces

3 interfaces between chains.

  • A–B · 882 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 650 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 633 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 2Z3N · complex structure of LF-transferase and peptide B · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A8P1 · AlphaFold monomer V2.0 prediction for LEUCYL/PHENYLALANYL-tRNA-- protein transferase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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