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Structure of L-asparaginase II precursor

Analyse Structure of L-asparaginase II precursor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WSA
Type: protein
Length: 639 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Asparagine amidohydrolase
EC: 3.5.1.1
UniProt: P50286
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Asparagine amidohydrolase (EC 3.5.1.1)	protein	319	33% helix, 20% strand	P50286
B	Asparagine amidohydrolase (EC 3.5.1.1)	protein	320	34% helix, 21% strand	P50286

Pockets

5 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	132	0.76	0.95	47	empty
2	228	0.50	0.76	27	empty
3	212	0.49	0.76	28	empty
4	57	0.32	0.77	19	empty
5	61	0.30	0.75	19	empty

Interfaces

1 interface between chains.

A–B · 2050 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

1WSA · Structure of L-asparaginase II precursor · the same entry in another collection · chain A against A, TM-score 1.00
P50286 · AlphaFold monomer V2.0 prediction for L-asparaginase (P50286) · 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 P50286
Elsewhere: RCSB PDB 1WSA · PDBe 1WSA · UniProt P50286

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