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Crystallographic structure of the circularly permuted human TASPASE1 protein

Analyse Crystallographic structure of the circularly permuted human TASPASE1 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VIN
Type: protein
Length: 728 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
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Threonine aspartase 1 (EC 3.4.25.-)	protein	364	33% helix, 24% strand	Q9H6P5

Pockets

7 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	893	0.77	0.80	83	empty
2	950	0.76	0.79	77	empty
3	79	0.55	0.87	22	empty
4	281	0.55	0.76	42	empty
5	62	0.51	0.86	23	empty

Interfaces

1 interface between chains.

A–B · 2120 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

6VIN · Crystallographic structure of the circularly permuted human Taspase1 protein · 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 A against A, TM-score 0.47

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 6VIN · PDBe 6VIN · UniProt Q9H6P5

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