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Cryo-EM structure of the deah-box helicase PRP2 in complex with its coactivator SPP2

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

PDB: 7DCR
Type: protein
Length: 711 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PRP2 isoform 1; Pre-mRNA-splicing factor SPP2
UniProt: A0A6A5Q5S8, A0A6A5Q6Y7
Pockets: 9 · best druggability 0.83

Structure

electron microscopy · 2 distinct chains · 37% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
x	PRP2 isoform 1	protein	653	38% helix, 16% strand	A0A6A5Q5S8
y	Pre-mRNA-splicing factor SPP2	protein	58	22% helix, 0% strand	A0A6A5Q6Y7

Pockets

9 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	679	0.83	0.87	87	empty
2	145	0.68	0.89	35	empty
3	104	0.61	0.88	26	empty
4	230	0.60	0.81	33	empty
5	219	0.48	0.75	30	empty

Interfaces

1 interface between chains.

x–y · 2163 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

7DCR · cryo-EM structure of the DEAH-box helicase Prp2 in complex with its coactivator Spp2 · the same entry in another collection · chain x against x, 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 A0A6A5Q5S8
Every structure of UniProt A0A6A5Q6Y7
Elsewhere: RCSB PDB 7DCR · PDBe 7DCR · UniProt A0A6A5Q5S8 · UniProt A0A6A5Q6Y7

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