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The crystal structure of the anti-viral APOBEC3G catalytic domain

Analyse The crystal structure of the anti-viral APOBEC3G catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3E1U
Type: protein
Length: 184 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA dc->du-editing enzyme apobec-3G
EC: 3.5.4.-
UniProt: Q9HC16
Ligands: ZN
Pockets: 2 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA dc->du-editing enzyme apobec-3G (EC 3.5.4.-)	protein	184	36% helix, 20% strand	Q9HC16

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	123	0.62	0.85	20	empty
2	94	0.40	0.77	21	empty

Compared structures

3E1U · The Crystal Structure of the Anti-Viral APOBEC3G Catalytic Domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9HC16 · AlphaFold monomer V2.0 prediction for DNA dc->du-editing enzyme apobec-3G (Q9HC16) · a predicted model of the same protein · chain A against A, TM-score 0.95

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9HC16
Elsewhere: RCSB PDB 3E1U · PDBe 3E1U · UniProt Q9HC16

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