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Human adenine phosphoribosyltransferase in apo and AMP complexed forms

Analyse Human adenine phosphoribosyltransferase in apo and AMP complexed forms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ZN9
Type
protein
Length
358 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Adenine phosphoribosyltransferase
EC
2.4.2.7
UniProt
P07741
Ligands
AMP
Pockets
2 · best druggability 0.67

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BAdenine phosphoribosyltransferase (EC 2.4.2.7)protein17935% helix, 35% strandP07741

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · chains 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, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14180.670.7932empty
23500.600.7730AMP

Interfaces

1 interface between chains.

  • A–B · 1570 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 1ZN9 · Human Adenine Phosphoribosyltransferase in Apo and AMP Complexed Forms · the same entry in another collection · chain A against A, TM-score 1.00
  • P07741 · AlphaFold monomer V2.0 prediction for adenine phosphoribosyltransferase (P07741) · a predicted model of the same protein · chain B against A, TM-score 0.99

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