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Crystal structure of a primate APOBEC3G N-terminal domain

Analyse Crystal structure of a primate APOBEC3G N-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5K82
Type
protein
Length
755 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Apolipoprotein B mRNA editing enzyme, catalytic peptide- like 3G,APOLIPOPROTEIN B mRNA…
UniProt
M1GSK9
Ligands
ZN
Pockets
7 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CApolipoprotein B mRNA editing enzyme, catalytic peptide- like 3G,APOLIPOPROTEIN B mRNA editing enzyme, catalytic peptide-like 3Gprotein18842% helix, 18% strandM1GSK9
DApolipoprotein B mRNA editing enzyme, catalytic peptide- like 3G,APOLIPOPROTEIN B mRNA editing enzyme, catalytic peptide-like 3Gprotein19140% helix, 17% strandM1GSK9

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains A, B, C, D

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

Pockets

7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1770.460.8217empty
2600.370.7917empty
31080.370.7422empty
4500.360.8018empty
5770.360.7612empty

Interfaces

3 interfaces between chains.

  • A–C · 753 Ų buried · 2 hydrogen bonds · protein-protein
  • B–D · 734 Ų buried · 1 hydrogen bond · protein-protein
  • A–B · 653 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 5K82 · Crystal Structure of a Primate APOBEC3G N-Terminal Domain · the same entry in another collection · chain A against A, TM-score 1.00

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