PDBsum entry 8xqr

Signaling protein

PDB id: 8xqr

Contents

Protein chains

240 a.a.

341 a.a.

57 a.a.

129 a.a.

279 a.a.

Ligands

FLF

PDB id:

8xqr

Name:

Signaling protein

Title:

Structure 2 of human class t gpcr tas2r14-minigs/gust complex with flufenamic acid.

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

Protein chain

P63092  (GNAS2_HUMAN) -  Guanine nucleotide-binding protein G(s) subunit alpha isoforms short from Homo sapiens

Seq: 394 a.a.

Struc: 240 a.a.*

Protein chain

P62873  (GBB1_HUMAN) -  Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 from Homo sapiens

Seq: 340 a.a.

Struc: 341 a.a.

Protein chain

P59768  (GBG2_HUMAN) -  Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 from Homo sapiens

Seq: 71 a.a.

Struc: 57 a.a.

Protein chain

No UniProt id for this chain

Struc: 129 a.a.

Protein chain

Q59310  (Q59310_CLOPF) -  exo-alpha-sialidase from Clostridium perfringens

Seq: 694 a.a.

Struc: 279 a.a.*

Protein chain

Q9NYV8  (T2R14_HUMAN) -  Taste receptor type 2 member 14 from Homo sapiens

Seq: 317 a.a.

Struc: 279 a.a.

* PDB and UniProt seqs differ at 271 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: Chain A: E.C.3.6.5.- - ?????
• Enzyme class 2: Chain R: E.C.3.2.1.18 - exo-alpha-sialidase.
• 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.

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.