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Crystal structure of human TASPASE1 (acivated form)

Analyse Crystal structure of human TASPASE1 (acivated form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2A8J
Type: protein
Length: 623 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Threonine aspartase 1
EC: 3.4.25.-
UniProt: Q9H6P5
Ligands: CL
Pockets: 9 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Threonine aspartase 1 (EC 3.4.25.-)	protein	310	30% helix, 31% strand	Q9H6P5
B	Threonine aspartase 1 (EC 3.4.25.-)	protein	313	29% helix, 30% strand	Q9H6P5

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	352	0.62	0.78	44	CL
2	332	0.61	0.78	50	CL
3	191	0.56	0.80	24	empty
4	85	0.50	0.84	23	empty
5	78	0.47	0.83	24	empty

Interfaces

1 interface between chains.

A–B · 2057 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

2A8J · Crystal Structure of human Taspase1 (acivated form) · the same entry in another collection · chain A against A, TM-score 1.00
Q9H6P5 · AlphaFold monomer V2.0 prediction for threonine aspartase 1 (Q9H6P5) · a predicted model of the same protein · chain B 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 Q9H6P5
Elsewhere: RCSB PDB 2A8J · PDBe 2A8J · UniProt Q9H6P5

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