MolNFT v1 · #159876 · protein

Crystal structure of full length APOBEC3G fkl

6P40 · Apolipoprotein B mRNA editing enzyme, catalytic peptide…: “Crystal structure of full length APOBEC3G fkl”. X-ray diffraction, 1 ligand (ZN), 7 pockets (best druggability 0.77). MolNFT v1 #159876 on GenesisL1: 3D structure, binding…

PDB: 6P40
Type: protein
Length: 728 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: 7 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Apolipoprotein B mRNA editing enzyme, catalytic peptide- like 3G	protein	364	38% helix, 24% strand	M1GSK9

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	362	0.77	0.87	51	empty
2	399	0.75	0.85	56	empty
3	641	0.71	0.79	75	empty
4	248	0.71	0.86	36	empty
5	206	0.57	0.79	23	empty

Interfaces

1 interface between chains.

A–B · 1878 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

6P40 · Crystal Structure of Full Length APOBEC3G FKL · 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 6P40 · PDBe 6P40 · UniProt M1GSK9

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