PDBsum entry 8xvh

Signaling protein

PDB id: 8xvh

Contents

Protein chains

233 a.a.

338 a.a.

57 a.a.

126 a.a.

21 a.a.

305 a.a.

PDB id:

8xvh

Name:

Signaling protein

Title:

Cryo-em structure of etbr bound with endothelin1

Structure:

Isoform gnas-2 of guanine nucleotide-binding protein g(s) subunit alpha isoforms short. 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.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: gnb1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Gene: gng2.

Authors:

J.Y.Hou,S.H.Liu,L.J.Wu,Z.J.Liu,T.Hua

Key ref:

J.Hou et al. (2024). Structural basis of antagonist selectivity in endothe receptors.. Cell discov, 10, 79. PubMed id: 39075075

Date:

15-Jan-24 Release date: 28-Aug-24

Protein chain

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

Seq: 394 a.a.

Struc: 233 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: 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: 71 a.a.

Struc: 57 a.a.

Protein chain

No UniProt id for this chain

Struc: 126 a.a.

Protein chain

P05305  (EDN1_HUMAN) -  Endothelin-1 from Homo sapiens

Seq: 212 a.a.

Struc: 21 a.a.

Protein chain

P24530  (EDNRB_HUMAN) -  Endothelin receptor type B from Homo sapiens

Seq: 442 a.a.

Struc: 305 a.a.

Protein chain

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

Seq: 694 a.a.

Struc: 305 a.a.*

* PDB and UniProt seqs differ at 293 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chain A: E.C.3.6.5.- - ?????
• Enzyme class 3: 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.