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PDBsum entry 8xqp

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protein ligands Protein-protein interface(s) links
Signaling protein PDB id
8xqp

 

 

 

 

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Contents
Protein chains
224 a.a.
338 a.a.
56 a.a.
286 a.a.
232 a.a.
Ligands
GOQ
CLR
PDB id:
8xqp
Name: Signaling protein
Title: Structure of human class t gpcr tas2r14-gustducin complex with aristolochic acid a.
Structure: Guanine nucleotide-binding protein g(t) subunit alpha-3. Chain: a. Engineered: yes. Guanine nucleotide-binding protein g(i)/g(s)/g(t) subunit beta-1. Chain: b. Synonym: transducin beta chain 1. Engineered: yes. Guanine nucleotide-binding protein g(i)/g(s)/g(o) subunit
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: gnb1. Gene: gng2. Clostridium perfringens, homo sapiens, synthetic construct.
Authors: X.L.Hu,L.J.Wu,T.Hua,Z.J.Liu
Key ref: X.Hu et al. Bitter taste tas2r14 activation by intracellular tast and cholesterol.. Nature, . PubMed id: 38776963
Date:
05-Jan-24     Release date:   10-Jul-24    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
A8MTJ3  (GNAT3_HUMAN) -  Guanine nucleotide-binding protein G(t) subunit alpha-3 from Homo sapiens
Seq:
Struc:
354 a.a.
224 a.a.*
Protein chain
P62873  (GBB1_HUMAN) -  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 from Homo sapiens
Seq:
Struc:
340 a.a.
338 a.a.
Protein chain
P59768  (GBG2_HUMAN) -  Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 from Homo sapiens
Seq:
Struc:
71 a.a.
56 a.a.
Protein chain
Q59310  (Q59310_CLOPF) -  exo-alpha-sialidase from Clostridium perfringens
Seq:
Struc:
 
Seq:
Struc:
694 a.a.
286 a.a.*
Protein chain
Q9NYV8  (T2R14_HUMAN) -  Taste receptor type 2 member 14 from Homo sapiens
Seq:
Struc:
317 a.a.
286 a.a.
Protein chain
No UniProt id for this chain
Struc: 232 a.a.
Key:    Secondary structure
* PDB and UniProt seqs differ at 304 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain R: E.C.3.2.1.18  - exo-alpha-sialidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.

 

 

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