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 4oli
Go to PDB code:
Transferase
PDB id
4oli
Loading ...
Contents
Protein chain
539 a.a.
Ligands
2TT
×2
Waters
×8
PDB id:
4oli
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Transferase
Title:
The pseudokinase/kinase protein from jak-family member tyk2
Structure:
Non-receptor tyrosine-protein kinase tyk2. Chain: a. Engineered: yes. Mutation: yes
Source:
Homo sapiens. Human. Organism_taxid: 9606. Gene: tyk2. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108
Resolution:
2.80Å
R-factor:
0.205
R-free:
0.257
Authors:
C.Eigenbrot,M.Ultsch,H.Wallweber
Key ref:
P.J.Lupardus et al. (2014). Structure of the pseudokinase-kinase domains from protein kinase TYK2 reveals a mechanism for Janus kinase (JAK) autoinhibition.
Proc Natl Acad Sci U S A
,
111
, 8025-8030.
PubMed id:
24843152
DOI:
10.1073/pnas.1401180111
Date:
23-Jan-14
Release date:
28-May-14
PROCHECK
Headers
References
Protein chain
?
P29597
(TYK2_HUMAN) - Non-receptor tyrosine-protein kinase TYK2 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1187 a.a.
539 a.a.
*
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 2 residue positions (black crosses)
Enzyme reactions
Enzyme class:
E.C.2.7.10.2
- non-specific protein-tyrosine kinase.
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
Reaction:
L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H
+
L-tyrosyl-[protein]
+
ATP
=
O-phospho-L-tyrosyl-[protein]
+
ADP
+
H(+)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
Added reference
DOI no:
10.1073/pnas.1401180111
Proc Natl Acad Sci U S A
111
:8025-8030 (2014)
PubMed id:
24843152
Structure of the pseudokinase-kinase domains from protein kinase TYK2 reveals a mechanism for Janus kinase (JAK) autoinhibition.
P.J.Lupardus,
M.Ultsch,
H.Wallweber,
P.Bir Kohli,
A.R.Johnson,
C.Eigenbrot.
ABSTRACT
No abstract given.
'); } }