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 2kbx
Go to PDB code:
Cell adhesion
PDB id
2kbx
Loading ...
Contents
Protein chains
171 a.a.
*
70 a.a.
*
Metals
_ZN
×2
*
Residue conservation analysis
PDB id:
2kbx
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
ProSAT
Name:
Cell adhesion
Title:
Solution structure of ilk-pinch complex
Structure:
Integrin-linked protein kinase. Chain: a. Fragment: n-terminal domain. Synonym: ilk-1, ilk-2, 59 kda serine/threonine-protein kinase, p59ilk. Engineered: yes. Lim and senescent cell antigen-like-containing domain protein 1. Chain: b.
Source:
Homo sapiens. Human. Organism_taxid: 9606. Gene: ilk, ilk1, ilk2. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: lims1, pinch, pinch1.
NMR struc:
20 models
Authors:
J.Qin
Key ref:
J.Qin Cytosketal proteins.
To be published
, .
Date:
10-Dec-08
Release date:
30-Dec-08
PROCHECK
Headers
References
Protein chain
?
Q13418
(ILK_HUMAN) - Scaffold protein ILK from Homo sapiens
Seq:
Struc:
452 a.a.
171 a.a.
Protein chain
?
P48059
(LIMS1_HUMAN) - LIM and senescent cell antigen-like-containing domain protein 1 from Homo sapiens
Seq:
Struc:
325 a.a.
70 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
Chain A:
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
'); } }