MolNFT v1 · #108720 · protein

Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation T232A, complexed with 2'-AMP

4WFR · 2',3'-cyclic-nucleotide 3'-phosphodiesterase: “Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation T232A, complexed with…”. X-ray diffraction, 1 ligand (2AM), 1 pocket (best druggability 0.54).…

PDB: 4WFR
Type: protein
Length: 204 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
Ligands: 2AM
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2',3'-cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37)	protein	204	30% helix, 31% strand	P16330

Ligands and binding sites

2AM · Adenosine-2'-monophosphate · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	254	0.54	0.77	37	2AM

Compared structures

4WFR · Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation… · 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 4WFR · PDBe 4WFR · UniProt P16330

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