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Crystal structure of circularly permuted human taspase-1

Analyse Crystal structure of circularly permuted human taspase-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UGK
Type: protein
Length: 620 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9H6P5
Ligands: NA, CL

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	316	—	Q9H6P5
B	—	protein	304	—	Q9H6P5

Ligands and binding sites

NA · Sodium ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 4 copies · chains A, B

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

Compared structures

6UGK · Crystal structure of circularly permuted human taspase-1 · 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 0.54

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 6UGK · PDBe 6UGK · UniProt Q9H6P5

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