Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 5k8s
Go to PDB code:
Transferase
PDB id
5k8s
Loading ...
Contents
Protein chains
146 a.a.
Ligands
CMP
×2
Waters
×356
PDB id:
5k8s
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Transferase
Title:
Camp bound pfpka-r (297-441)
Structure:
Camp-dependent protein kinase regulatory subunit. Chain: a, b. Fragment: unp residues 297-441. Engineered: yes
Source:
Plasmodium falciparum (isolate 3d7). Organism_taxid: 36329. Strain: isolate 3d7. Gene: pkar, pfl1110c. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.15Å
R-factor:
0.199
R-free:
0.218
Authors:
D.R.Littler,P.R.Gilson,B.S.Crabb,J.J.Rossjohn
Key ref:
D.R.Littler et al. (2016). Disrupting the Allosteric Interaction between the Plasmodium falciparum cAMP-dependent Kinase and Its Regulatory Subunit.
J Biol Chem
,
291
, 25375-25386.
PubMed id:
27738107
DOI:
10.1074/jbc.M116.750174
Date:
31-May-16
Release date:
12-Oct-16
PROCHECK
Headers
References
Protein chains
?
Q7KQK0
(Q7KQK0_PLAF7) - cAMP-dependent protein kinase regulatory subunit from Plasmodium falciparum (isolate 3D7)
Seq:
Struc:
441 a.a.
146 a.a.
*
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 3 residue positions (black crosses)
Enzyme reactions
Enzyme class:
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 =
CMP
)
matches with 81.48% similarity
+
ADP
+
H(+)
L-threonyl-[protein]
+
ATP
=
O-phospho-L-threonyl-[protein]
Bound ligand (Het Group name =
CMP
)
matches with 81.48% similarity
+
ADP
+
H(+)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
reference
DOI no:
10.1074/jbc.M116.750174
J Biol Chem
291
:25375-25386 (2016)
PubMed id:
27738107
Disrupting the Allosteric Interaction between the Plasmodium falciparum cAMP-dependent Kinase and Its Regulatory Subunit.
D.R.Littler,
H.E.Bullen,
K.L.Harvey,
T.Beddoe,
B.S.Crabb,
J.Rossjohn,
P.R.Gilson.
ABSTRACT
No abstract given.
'); } }