MolNFT v1 · #53144 · protein

The crystal structure of helicobacter pylori L-asparaginase at 1.4 a resolution

2WLT: “The crystal structure of helicobacter pylori L-asparaginase at 1.4 a resolution”. X-ray diffraction, 1 ligand (ASP), 2 pockets (best druggability 0.40). MolNFT v1 #53144 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2WLT
Type: protein
Length: 326 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-asparaginase
EC: 3.5.1.1
UniProt: Q9ZLB9
Ligands: ASP
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-asparaginase (EC 3.5.1.1)	protein	326	33% helix, 21% strand	Q9ZLB9

Ligands and binding sites

ASP · Aspartic acid · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.40	0.81	16	empty
2	55	0.39	0.81	22	empty

Compared structures

2WLT · The crystal structure of Helicobacter pylori L-asparaginase at 1.4 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
Q9ZLB9 · AlphaFold monomer V2.0 prediction for probable L-asparaginase (Q9ZLB9) · a predicted model of the same protein · chain A against A, TM-score 1.00

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 Q9ZLB9
Elsewhere: RCSB PDB 2WLT · PDBe 2WLT · UniProt Q9ZLB9

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