PDBsum entry 9chx

Membrane protein/hydrolase/isomerase

PDB id: 9chx

Contents

Protein chains

432 a.a.

350 a.a.

107 a.a.

Ligands

CAU

FK5

PDB id:

9chx

Name:

Membrane protein/hydrolase/isomerase

Title:

Cryo-em structure of calcineurin-fused beta2 adrenergic receptor in carazolol bound inactive state

Structure:

Beta-2 adrenergic receptor,calcineurin subunit b type 1. Chain: a. Engineered: yes. Other_details: residues 29-354 (uniprot numbering) of the beta2-ar with the third cytoplasmic domain replaced with residues 16-170 (uniprot numbering) of calcineurin subunit b. Protein phosphatase 3 catalytic subunit alpha. Chain: b. Fragment: residues 1-370.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: adrb2, adrb2r, b2ar, ppp3r1, cna2, cnb. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Mus musculus. House mouse. Organism_taxid: 10090.

Authors:

J.Xu,G.Chen,Y.Du,B.K.Kobilka

Key ref:

J.Xu et al. (2024). Calcineurin-Fusion facilitates cryo-Em structure determination of a family a gpcr.. Proc natl acad sci usa, 121, 44121. PubMed id: 39565314

Date:

02-Jul-24 Release date: 13-Nov-24

Protein chain

P07550  (ADRB2_HUMAN) -  Beta-2 adrenergic receptor from Homo sapiens

Seq: 413 a.a.

Struc: 432 a.a.*

Protein chain

P63098  (CANB1_HUMAN) -  Calcineurin subunit B type 1 from Homo sapiens

Seq: 170 a.a.

Struc: 432 a.a.*

Protein chain

P63328  (PP2BA_MOUSE) -  Protein phosphatase 3 catalytic subunit alpha from Mus musculus

Seq: 521 a.a.

Struc: 350 a.a.

Protein chain

P62942  (FKB1A_HUMAN) -  Peptidyl-prolyl cis-trans isomerase FKBP1A from Homo sapiens

Seq: 108 a.a.

Struc: 107 a.a.

* PDB and UniProt seqs differ at 154 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chain B: E.C.3.1.3.16 - protein-serine/threonine phosphatase.
• Reaction:
  1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
  2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate
• Enzyme class 3: Chain C: E.C.5.2.1.8 - peptidylprolyl isomerase.
• Reaction: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)

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.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site