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Perdeuterated mouse cnpase catalytic domain at atomic resolution

Analyse Perdeuterated mouse cnpase catalytic domain at atomic resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AE0
Type: protein
Length: 217 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: CL
Pockets: 2 · best druggability 0.60

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2', 3'-cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37)	protein	217	31% helix, 30% strand	P16330

Ligands and binding sites

CL · Chloride ion · ion · chains A
CIT · Citric acid · additive · chains A

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

Pockets

2 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	331	0.60	0.78	40	CL
2	60	0.37	0.78	13	empty

Compared structures

5AE0 · Perdeuterated mouse CNPase catalytic domain at atomic resolution · 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 0.95

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 P16330
Elsewhere: RCSB PDB 5AE0 · PDBe 5AE0 · UniProt P16330

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