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PDBsum entry 5awm
Go to PDB code:
Transferase
PDB id
5awm
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Contents
Protein chain
345 a.a.
Ligands
ANP
Metals
_MG
×2
Waters
×143
PDB id:
5awm
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Transferase
Title:
The crystal structure of jnk from drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian jnk proteins.
Structure:
Stress-activated protein kinase jnk. Chain: a. Synonym: djnk,protein basket. Engineered: yes
Source:
Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: bsk, jnk, cg5680. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.79Å
R-factor:
0.179
R-free:
0.220
Authors:
P.Boonserm
Key ref:
S.Chimnaronk et al. (2015). The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteins.
Bmc Struct Biol
,
15
, 17.
PubMed id:
26377800
DOI:
10.1186/s12900-015-0045-1
Date:
06-Jul-15
Release date:
05-Aug-15
Supersedes:
4m3a
PROCHECK
Headers
References
Protein chain
?
P92208
(JNK_DROME) - Stress-activated protein kinase JNK from Drosophila melanogaster
Seq:
Struc:
372 a.a.
345 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
E.C.2.7.11.24
- mitogen-activated 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]
+
ADP
Bound ligand (Het Group name =
ANP
)
matches with 81.25% similarity
+
H(+)
L-threonyl-[protein]
+
ATP
=
O-phospho-L-threonyl-[protein]
+
ADP
Bound ligand (Het Group name =
ANP
)
matches with 81.25% similarity
+
H(+)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
reference
DOI no:
10.1186/s12900-015-0045-1
Bmc Struct Biol
15
:17 (2015)
PubMed id:
26377800
The crystal structure of JNK from Drosophila melanogaster reveals an evolutionarily conserved topology with that of mammalian JNK proteins.
S.Chimnaronk,
J.Sitthiroongruang,
K.Srisucharitpanit,
M.Srisaisup,
A.J.Ketterman,
P.Boonserm.
ABSTRACT
No abstract given.
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