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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: 6FA5
Type: protein
Length: 635 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
Pockets: 8 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative mRNA splicing factor	protein	635	43% helix, 18% strand	G0SEG4

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	695	0.83	0.87	82	empty
2	152	0.70	0.89	23	empty
3	469	0.68	0.79	63	ADP, MG
4	97	0.46	0.80	23	empty
5	52	0.46	0.85	17	empty

Compared structures

6FA5 · 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 6FA5 · PDBe 6FA5 · UniProt G0SEG4

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