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Crystal structure of DCP1P

Analyse Crystal structure of DCP1P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q67
Type: protein
Length: 307 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Decapping protein involved in mRNA degradation- DCP1P
UniProt: Q12517
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Decapping protein involved in mRNA degradation- DCP1P	protein	146	27% helix, 42% strand	Q12517
B	Decapping protein involved in mRNA degradation- DCP1P	protein	161	22% helix, 39% strand	Q12517

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	131	0.70	0.91	26	empty
2	72	0.32	0.75	18	empty
3	77	0.31	0.74	16	empty
4	50	0.27	0.74	14	empty
5	51	0.26	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 861 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1Q67 · Crystal structure of Dcp1p · the same entry in another collection · chain A against A, TM-score 1.00
Q12517 · AlphaFold monomer V2.0 prediction for mRNA-decapping enzyme subunit 1 (Q12517) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 Q12517
Elsewhere: RCSB PDB 1Q67 · PDBe 1Q67 · UniProt Q12517

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