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 6z4z
Go to PDB code:
Transferase
PDB id
6z4z
Loading ...
Contents
Protein chains
337 a.a.
Ligands
PO4
×4
GOL
PQ5
×3
Waters
×418
PDB id:
6z4z
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Transferase
Title:
Crystal structure of clk1 in complex with macrocycle ods2004070
Structure:
Dual specificity protein kinase clk1. Chain: a, b, c. Synonym: cdc-like kinase 1. Engineered: yes
Source:
Homo sapiens. Human. Organism_taxid: 9606. Gene: clk1, clk. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: -r3-prare2.
Resolution:
2.07Å
R-factor:
0.177
R-free:
0.213
Authors:
A.Chaikuad,P.Benderitter,J.Hoflack,A.Denis,S.Knapp,Structural Genomics Consortium (Sgc)
Key ref:
A.Chaikuad et al. Crystal structure of clk1 in complex with macrocycle ods2004070.
To be published
, .
Date:
26-May-20
Release date:
03-Jun-20
PROCHECK
Headers
References
Protein chains
?
P49759
(CLK1_HUMAN) - Dual specificity protein kinase CLK1 from Homo sapiens
Seq:
Struc:
484 a.a.
337 a.a.
*
Key:
PfamA domain
Secondary structure
*
PDB and UniProt seqs differ at 3 residue positions (black crosses)
Enzyme reactions
Enzyme class:
E.C.2.7.12.1
- dual-specificity 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
+
3.
L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[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(+)
L-tyrosyl-[protein]
+
ATP
=
O-phospho-L-tyrosyl-[protein]
+
ADP
+
H(+)
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
'); } }