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PDBsum entry 6y8c
Go to PDB code:
Transferase
PDB id
6y8c
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Contents
Protein chains
339 a.a.
18 a.a.
Ligands
ATP
DMS
×5
MPD
×2
Metals
_MG
Waters
×305
PDB id:
6y8c
Links
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CATH
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ProSAT
Name:
Transferase
Title:
Crystal structure of the camp-dependent protein kinase a cocrystallized with atp and pki (5-24)
Structure:
Camp-dependent protein kinase catalytic subunit alpha. Chain: a. Synonym: pka c-alpha. Engineered: yes. Camp-dependent protein kinase inhibitor alpha. Chain: b. Synonym: pki-alpha,camp-dependent protein kinase inhibitor, muscle/brain isoform. Engineered: yes
Source:
Cricetulus griseus. Chinese hamster. Organism_taxid: 10029. Gene: prkaca. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Mus musculus. Mouse.
Resolution:
1.76Å
R-factor:
0.162
R-free:
0.190
Authors:
M.Oebbeke,A.Heine,G.Klebe
Key ref:
M.Oebbeke et al. A crystallographic study of camp-Dependent protein ki in complex with different fasudil-Derivatives.
To be published
, .
Date:
04-Mar-20
Release date:
30-Sep-20
PROCHECK
Headers
References
Protein chain
?
P25321
(KAPCA_CRIGR) - cAMP-dependent protein kinase catalytic subunit alpha from Cricetulus griseus
Seq:
Struc:
351 a.a.
339 a.a.
*
Protein chain
?
P63248
(IPKA_MOUSE) - cAMP-dependent protein kinase inhibitor alpha from Mus musculus
Seq:
Struc:
76 a.a.
18 a.a.
Key:
PfamA domain
Secondary structure
*
PDB and UniProt seqs differ at 1 residue position (black cross)
Enzyme reactions
Enzyme class:
Chain A:
E.C.2.7.11.11
- cAMP-dependent protein kinase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
1.
L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H
+
2.
L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H
+
L-seryl-[protein]
+
ATP
=
O-phospho-L-seryl-[protein]
Bound ligand (Het Group name =
ATP
)
corresponds exactly
+
ADP
+
H(+)
L-threonyl-[protein]
+
ATP
=
O-phospho-L-threonyl-[protein]
Bound ligand (Het Group name =
ATP
)
corresponds exactly
+
ADP
+
H(+)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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