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PDBsum entry 8xqp
Go to PDB code:
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
Links
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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
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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