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The crystal structure of novel APOBEC3G CD2 head-to-tail dimer suggests the binding mode of full-length APOBEC3G to HIV-1 ssdna

Analyse The crystal structure of novel APOBEC3G CD2 head-to-tail dimer suggests the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ROW
Type: protein
Length: 191 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: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA dc->du-editing enzyme apobec-3G (EC 3.5.4.-)	protein	191	38% helix, 21% 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	72	0.37	0.77	14	empty

Compared structures

4ROW · The crystal structure of novel APOBEC3G CD2 head-to-tail dimer suggests the binding mode… · 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 0.96

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 4ROW · PDBe 4ROW · UniProt Q9HC16

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