Research workbench

Solution structure of C-terminal domain of APOBEC3G

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

PDB: 2JYW
Type: protein
Length: 187 residues
Chains: 1
Method: solution nmr
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: 3 · best druggability 0.43

Structure

solution nmr · 1 distinct chain · 33% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA dc->du-editing enzyme apobec-3G (EC 3.5.4.-)	protein	187	33% helix, 17% 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	136	0.43	0.75	20	empty
2	67	0.36	0.77	14	empty
3	57	0.30	0.75	18	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2JYW · Solution structure of C-terminal domain of APOBEC3G · 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 0.68

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 2JYW · PDBe 2JYW · UniProt Q9HC16

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.