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Solution structure of catalytic domain of YDCP2

Analyse Solution structure of catalytic domain of YDCP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2JVB
Type: protein
Length: 146 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MRNA-decapping enzyme subunit 2
EC: 3.-.-.-
UniProt: P53550
Pockets: 1 · best druggability 0.63

Structure

solution nmr · 1 distinct chain · 27% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MRNA-decapping enzyme subunit 2 (EC 3.-.-.-)	protein	146	27% helix, 23% strand	P53550

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	177	0.63	0.84	35	empty

Compared structures

2JVB · Solution Structure of Catalytic Domain of yDcp2 · the same entry in another collection · chain A against A, TM-score 1.00
P53550 · AlphaFold monomer V2.0 prediction for M7GPPPN-mRNA hydrolase (P53550) · a predicted model of the same protein · chain A against A, TM-score 0.81

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 P53550
Elsewhere: RCSB PDB 2JVB · PDBe 2JVB · UniProt P53550

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