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 3gu4
Go to PDB code:
Transferase
PDB id
3gu4
Loading ...
Contents
Protein chain
280 a.a.
*
Ligands
ANP
Waters
×338
*
Residue conservation analysis
PDB id:
3gu4
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Transferase
Title:
Crystal structure of dapkq23v-amppnp
Structure:
Death-associated protein kinase 1. Chain: a. Fragment: protein kinase domain. Synonym: dap kinase 1. Engineered: yes. Mutation: yes
Source:
Homo sapiens. Human. Organism_taxid: 9606. Gene: dapk, dapk1, death-associated protein kinase 1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.35Å
R-factor:
0.185
R-free:
0.211
Authors:
L.K.Mcnamara,J.S.Schavocky,D.M.Watterson,J.S.Brunzelle
Key ref:
L.K.Mcnamara et al. Enzymatic activity and crystallgoraphic analyses of a glycine-Rich loop mutant of dapk.
To be published
, .
Date:
28-Mar-09
Release date:
09-Mar-10
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.
280 a.a.
*
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 5 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]
Bound ligand (Het Group name =
ANP
)
matches with 81.25% similarity
+
ADP
+
H(+)
L-threonyl-[protein]
+
ATP
=
O-phospho-L-threonyl-[protein]
Bound ligand (Het Group name =
ANP
)
matches with 81.25% similarity
+
ADP
+
H(+)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
'); } }