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Crystal structure of the RNA-helicase PRP28 from chaetomium thermophilum bound to ADP

Analyse Crystal structure of the RNA-helicase PRP28 from chaetomium thermophilum bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5DTU
Type: protein
Length: 404 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PRP28
UniProt: G0SBQ7
Ligands: ADP, MG
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	PRP28	protein	404	37% helix, 15% strand	G0SBQ7

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	733	0.73	0.79	79	empty
2	154	0.63	0.85	23	empty
3	156	0.45	0.75	21	empty
4	67	0.36	0.77	18	empty
5	80	0.30	0.73	19	empty

Compared structures

5DTU · Crystal structure of the RNA-helicase Prp28 from Chaetomium thermophilum bound to 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 G0SBQ7
Elsewhere: RCSB PDB 5DTU · PDBe 5DTU · UniProt G0SBQ7

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