Research workbench

Crystal structure of the deah-box helicase PRP2 in complex with ADP

Analyse Crystal structure of the deah-box helicase PRP2 in complex with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FAC
Type: protein
Length: 653 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative mRNA splicing factor
UniProt: G0SEG4
Ligands: ADP, MG, CL
Pockets: 6 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative mRNA splicing factor	protein	653	46% helix, 19% strand	G0SEG4

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 4 copies · chains A

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

Pockets

6 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	938	0.83	0.84	99	CL
2	191	0.67	0.86	25	empty
3	352	0.66	0.81	42	ADP, MG
4	224	0.51	0.76	26	empty
5	201	0.45	0.74	29	empty

Compared structures

6FAC · Crystal structure of the deah-box helicase PRP2 in complex with ADP · 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 G0SEG4
Elsewhere: RCSB PDB 6FAC · PDBe 6FAC · UniProt G0SEG4

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