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 1v5s
Go to PDB code:
Transferase
PDB id
1v5s
Loading ...
Contents
Protein chain
126 a.a.
*
*
Residue conservation analysis
PDB id:
1v5s
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
ProSAT
Name:
Transferase
Title:
Solution structure of kinase associated domain 1 of mouse map/microtubule affinity-regulating kinase 3
Structure:
Map/microtubule affinity-regulating kinase 3. Chain: a. Fragment: kinase associated domain 1. Engineered: yes
Source:
Mus musculus. House mouse. Organism_taxid: 10090. Gene: riken cdna 1600015g02. Other_details: cell-free protein synthesis
NMR struc:
20 models
Authors:
N.Tochio,S.Koshiba,M.Inoue,T.Kigawa,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref:
N.Tochio et al. Solution structure of kinase associated domain 1 of mouse map/microtubule affinity-Regulating kinase 3.
To be published
, .
Date:
25-Nov-03
Release date:
25-May-04
PROCHECK
Headers
References
Protein chain
?
Q03141
(MARK3_MOUSE) - MAP/microtubule affinity-regulating kinase 3 from Mus musculus
Seq:
Struc:
 
Seq:
Struc:
753 a.a.
126 a.a.
*
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 36 residue positions (black crosses)
Enzyme reactions
Enzyme class:
E.C.2.7.11.1
- non-specific serine/threonine 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
+
H(+)
L-threonyl-[protein]
+
ATP
=
O-phospho-L-threonyl-[protein]
+
ADP
+
H(+)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
'); } }