3IXE: Integrin-linked protein kinase

Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase. Determined by X-ray diffraction at 1.9 Å resolution. Released 15 Dec 2009.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,370
Mol. weight: 28.87 kDa
Ligands: ZN
Released: 15 Dec 2009

Explore 3IXE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3IXE contains 14 α-helices and 8 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	4-10	7
α-helix	13-21	9
α-helix	37-43	7
α-helix	47-55	9
α-helix	70-76	7
α-helix	80-88	9
α-helix	103-109	7
α-helix	113-121	9
β-strand	128	1	1
α-helix	136-139	4
α-helix	142-154	13
β-strand	162	1	1

Chain B: 4 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	9	1	2
β-strand	16	1	2
α-helix	22-23	2
β-strand	24-26	3	3
β-strand	29-31	3	3
α-helix	43-45	3
α-helix	46-48	3
β-strand	51-53	3	4
β-strand	56-58	3	4
α-helix	60-66	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Integrin-linked protein kinase	A	protein	179	Homo sapiens	Q13418 (AlphaFold model)
LIM and senescent cell antigen-like-containing domain protein 2	B	protein	72	Homo sapiens	Q7Z4I7 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3IXE_1 Integrin-linked protein kinase (chains A)
GSPEFMDDIFTQCREGNAVAVRLWLDNTENDLNQGDDHGFSPLHWACREGRSAVVEMLIM
RGARINVMNRGDDTPLHLAASHGHRDIVQKLLQYKADINAVNEHGNVPLHYACFWGQDQV
AEDLVANGALVSICNKYGEMPVDKAKAPLRELLRERAEKMGQNLNRIPYKDTFWKGTTR

Sequence of entity 2 (B), FASTA

>3IXE_2 LIM and senescent cell antigen-like-containing domain protein 2 (chains B)
SENLYFQGSANAVCQRCQARFSPAERIVNSNGELYHEHCFVCAQCFRPFPEGLFYEFEGR
KYCEHDFQMLFA

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Primary citation

Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase. Chiswell, B.P., Stiegler, A.L., Razinia, Z. et al. J Struct Biol (2010) 170:157-163. DOI 10.1016/j.jsb.2009.12.002 · PubMed

Other PDB entries of the same protein (UniProt Q13418 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4HI8 1.2 Å, Structure of integrin-linked kinase ankyrin repeat domain in complex with PINCH1 LIM1…
4HI9 1.2 Å, 1.2 structure of integrin-linked kinase ankyrin repeat domain in complex with PINCH1…
9TP9 1.45 Å, Crystal structure of integrin-linked kinase (ILK) in complex with Alpha-Parvin and…
9D5E 1.5 Å, Crystal structure of the ILK/alpha-parvin core complex bound to gefitinib
9D5F 1.5 Å, Crystal structure of the ILK/alpha-parvin core complex bound to bosutinib
9D5H 1.5 Å, Crystal structure of the ILK mutant (R371Q)/alpha-parvin core complex bound to gefitinib
9D5I 1.5 Å, Crystal structure of the ILK mutant (R225A)/alpha-parvin core complex bound to MgATP
9D5P 1.5 Å, Crystal structure of the ILK/alpha-parvin core complex bound to erlotinib
9TPD 1.5 Å, Crystal structure of integrin-linked kinase (ILK) in complex with alpha-parvin and a…
9D5G 1.55 Å, Crystal structure of the ILK/alpha-parvin core complex bound to 4-methyl erlotinib
3F6Q 1.6 Å, Crystal structure of integrin-linked kinase ankyrin repeat domain in complex with PINCH1…
3KMU 1.8 Å, Crystal structure of the ILK/alpha-parvin core complex (apo)

Browse structure collections

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