Research workbench

Asymmetric trimer of the human DCP1A C-terminal domain

Analyse Asymmetric trimer of the human DCP1A C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WX3
Type: protein
Length: 132 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MRNA-decapping enzyme 1A
UniProt: Q9NPI6

Structure

x-ray diffraction · 3 distinct chains · 73% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MRNA-decapping enzyme 1A	protein	43	84% helix, 0% strand	Q9NPI6
B	MRNA-decapping enzyme 1A	protein	42	69% helix, 0% strand	Q9NPI6
C	MRNA-decapping enzyme 1A	protein	47	68% helix, 0% strand	Q9NPI6

Interfaces

3 interfaces between chains.

B–C · 1108 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 984 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 918 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

2WX3 · Asymmetric trimer of the human DCP1a C-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9NPI6 · AlphaFold monomer V2.0 prediction for mRNA-decapping enzyme 1A (Q9NPI6) · a predicted model of the same protein · chain C against A, TM-score 0.76

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 Q9NPI6
Elsewhere: RCSB PDB 2WX3 · PDBe 2WX3 · UniProt Q9NPI6

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