MolNFT v1 · #78662 · protein

Crystal structure of full-length murine apaf-1

3SFZ · Apoptotic peptidase activating factor 1: “Crystal structure of full-length murine apaf-1”. X-ray diffraction, 2 ligands (GBL, ADP), 12 pockets (best druggability 0.85). MolNFT v1 #78662 on GenesisL1: 3D structure, binding sites and…

PDB: 3SFZ
Type: protein
Length: 1,133 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apoptotic peptidase activating factor 1
UniProt: A2RRK8
Ligands: GBL, ADP
Pockets: 12 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Apoptotic peptidase activating factor 1	protein	1133	23% helix, 28% strand	A2RRK8

Ligands and binding sites

GBL · Gamma-butyrolactone · ligand · 5 copies · chains A
ADP · Adenosine-5'-diphosphate · ligand · chains A

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

Pockets

12 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	996	0.85	0.86	105	ADP, GBL
2	591	0.75	0.82	49	empty
3	1010	0.73	0.76	65	empty
4	472	0.68	0.79	63	empty
5	444	0.68	0.79	64	GBL

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

3SFZ · Crystal structure of full-length murine Apaf-1 · 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 A2RRK8
Elsewhere: RCSB PDB 3SFZ · PDBe 3SFZ · UniProt A2RRK8

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