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Ligand free type II E. COLI asparaginase T12S/T89S double mutant

Analyse Ligand free type II E. COLI asparaginase T12S/T89S double mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7A0U
Type: protein
Length: 1,255 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-asparaginase 2
EC: 3.5.1.1
UniProt: P00805
Pockets: 17 · best druggability 0.71

Structure

x-ray diffraction · 4 distinct chains · 33% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L-asparaginase 2 (EC 3.5.1.1)	protein	316	33% helix, 22% strand	P00805
B	L-asparaginase 2 (EC 3.5.1.1)	protein	326	33% helix, 21% strand	P00805
C	L-asparaginase 2 (EC 3.5.1.1)	protein	308	32% helix, 22% strand	P00805
D	L-asparaginase 2 (EC 3.5.1.1)	protein	305	32% helix, 22% strand	P00805

Pockets

17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.71	0.97	23	empty
2	610	0.69	0.78	49	empty
3	311	0.57	0.77	37	empty
4	270	0.54	0.76	32	empty
5	230	0.51	0.76	28	empty

Interfaces

4 interfaces between chains.

A–C · 2060 Å² buried · 39 hydrogen bonds · protein-protein
B–D · 282 Å² buried · 5 hydrogen bonds · protein-protein
A–D · 260 Å² buried · 0 hydrogen bonds · protein-protein
B–C · 244 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

7A0U · Ligand free type II E. COLI asparaginase T12S/T89S double mutant · the same entry in another collection · chain D against D, TM-score 1.00
P00805 · AlphaFold monomer V2.0 prediction for L-asparaginase 2 (P00805) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 P00805
Elsewhere: RCSB PDB 7A0U · PDBe 7A0U · UniProt P00805

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