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PDBsum entry 4c4k
Go to PDB code:
Transferase
PDB id
4c4k
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Contents
Protein chains
94 a.a.
97 a.a.
Ligands
EDO
×12
Waters
×114
PDB id:
4c4k
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Transferase
Title:
Crystal structure of the titin m10-obscurin ig domain 1 complex
Structure:
Obscurin. Chain: o. Fragment: first ig domain, residues 9-103. Synonym: obscurin-rhogef, obscurin-myosin light chain kinase, obscurin-mlck. Engineered: yes. Titin. Chain: t. Fragment: m10 domain, residues 34252-34350.
Source:
Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta 2.
Resolution:
1.95Å
R-factor:
0.173
R-free:
0.210
Authors:
S.Pernigo,A.Fukuzawa,M.Gautel,R.A.Steiner
Key ref:
S.Pernigo et al. (2015). The crystal structure of the human titin:obscurin complex reveals a conserved yet specific muscle M-band zipper module.
J Mol Biol
,
427
, 718-736.
PubMed id:
25490259
DOI:
10.1016/j.jmb.2014.11.019
Date:
05-Sep-13
Release date:
24-Sep-14
PROCHECK
Headers
References
Protein chain
Q5VST9
(OBSCN_HUMAN) - Obscurin from Homo sapiens
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7968 a.a.
94 a.a.
*
Protein chain
?
Q8WZ42
(TITIN_HUMAN) - Titin from Homo sapiens
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34350 a.a.
97 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
*
PDB and UniProt seqs differ at 1 residue position (black cross)
Enzyme reactions
Enzyme class:
Chains O, T:
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
reference
DOI no:
10.1016/j.jmb.2014.11.019
J Mol Biol
427
:718-736 (2015)
PubMed id:
25490259
The crystal structure of the human titin:obscurin complex reveals a conserved yet specific muscle M-band zipper module.
S.Pernigo,
A.Fukuzawa,
A.Pandini,
M.Holt,
J.Kleinjung,
M.Gautel,
R.A.Steiner.
ABSTRACT
No abstract given.
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