MolNFT v1 · #159873 · protein

Crystal structure of full length APOBEC3G E/Q (pH 7.0)

6P3X · Apolipoprotein B mRNA editing enzyme, catalytic peptide…: “Crystal structure of full length APOBEC3G E/Q (pH 7.0)”. X-ray diffraction, 1 ligand (ZN), 9 pockets (best druggability 0.59). MolNFT v1 #159873 on GenesisL1: 3D structure…

PDB: 6P3X
Type: protein
Length: 724 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apolipoprotein B mRNA editing enzyme, catalytic peptide- like 3G
UniProt: M1GSK9
Ligands: ZN
Pockets: 9 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Apolipoprotein B mRNA editing enzyme, catalytic peptide- like 3G	protein	362	40% helix, 23% strand	M1GSK9

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	216	0.59	0.80	33	empty
2	209	0.57	0.79	32	empty
3	170	0.52	0.79	27	empty
4	148	0.52	0.79	25	empty
5	222	0.48	0.75	25	empty

Interfaces

1 interface between chains.

A–B · 707 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

6P3X · Crystal Structure of Full Length APOBEC3G E/Q (pH 7.0) · the same entry in another collection · chain A against A, TM-score 1.00

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 M1GSK9
Elsewhere: RCSB PDB 6P3X · PDBe 6P3X · UniProt M1GSK9

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