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 1wvx
Go to PDB code:
Transferase
PDB id
1wvx
Loading ...
Contents
Protein chain
275 a.a.
*
Ligands
BD4
Waters
×74
*
Residue conservation analysis
PDB id:
1wvx
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
CSA
PROCOGNATE
ProSAT
Name:
Transferase
Title:
Crystal structures of kinase domain of dap kinase in complex with small molecular inhibitors
Structure:
Death-associated protein kinase 1. Chain: a. Fragment: catalytic domain. Synonym: dap kinase 1. Engineered: yes
Source:
Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.60Å
R-factor:
0.225
R-free:
0.270
Authors:
Y.Ueda,H.Ogata,A.Yamakawa,Y.Higuchi
Key ref:
Y.Ueda et al. Complex structure of kinase domain of dap kinase with bdb402.
To be published
, .
Date:
27-Dec-04
Release date:
11-Apr-06
PROCHECK
Headers
References
Protein chain
?
P53355
(DAPK1_HUMAN) - Death-associated protein kinase 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1430 a.a.
275 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
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
'); } }