MolNFT v1 · #108589 · protein

Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutations H230Q and H309Q

4WBI · 2',3'-cyclic-nucleotide 3'-phosphodiesterase: “Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutations H230Q and H309Q”. X-ray diffraction, 1 pocket (best druggability 0.55). MolNFT v1 #108589 on…

PDB: 4WBI
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2',3'-cyclic-nucleotide 3'-phosphodiesterase
EC: 3.1.4.37
UniProt: P16330
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2',3'-cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37)	protein	208	31% helix, 32% strand	P16330

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	253	0.55	0.77	37	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

4WBI · Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutations… · the same entry in another collection · chain A against A, TM-score 1.00
P16330 · AlphaFold monomer V2.0 prediction for 2',3'-cyclic-nucleotide 3'-phosphodiesterase… · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P16330
Elsewhere: RCSB PDB 4WBI · PDBe 4WBI · UniProt P16330

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