3KMW: ILK/alpha-parvin core complex

Crystal structure of the ILK/alpha-parvin core complex (MgATP). Determined by X-ray diffraction at 2.0 Å resolution. Released 29 Dec 2009.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,498
Mol. weight: 46.35 kDa
Ligands: ATP, MG
Released: 29 Dec 2009

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

Secondary structure: helices and β-sheets

3KMW contains 27 α-helices and 11 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: 20 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	190-192	3
β-strand	194-202	9	1
β-strand	205-212	8	1
β-strand	215-222	8	1
α-helix	223	1
α-helix	229-238	10
α-helix	239-242	4
β-strand	250-251	2	2
β-strand	253-257	5	1
β-strand	266-270	5	1
β-strand	276	1	2
α-helix	277-282	6
α-helix	291-308	18
α-helix	314-315	2
α-helix	322-324	3
β-strand	325-327	3	2
β-strand	333-336	4	2
α-helix	337-339	3
α-helix	341-342	2
β-strand	350	1	3
α-helix	353-355	3
α-helix	358-362	5
α-helix	365-367	3
α-helix	370-387	18
α-helix	397-406	10
α-helix	411-414	4
α-helix	419-428	10
α-helix	433-435	3
α-helix	437-438	2
α-helix	439-450	12

Chain B: 7 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	250-256	7
α-helix	258-277	20
α-helix	294-304	11
β-strand	307	1	3
α-helix	310-312	3
α-helix	320-336	17
α-helix	346-350	5
α-helix	354-367	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Integrin-linked kinase	A	protein	271	Homo sapiens	Q13418 (AlphaFold model)
Alpha-parvin	B	protein	129	Homo sapiens	Q9NVD7 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3KMW_1 Integrin-linked kinase (chains A)
MNKHSGIDFKQLNFLTKLNENHSGELWKGRWQGNDIVVKVLKVRDWSTRKSRDFNEECPR
LRIFSHPNVLPVLGACQSPPAPHPTLITHWMPYGSLYNVLHEGTNFVVDQSQAVKFALDM
ARGMAFLHTLEPLIPRHALNSRSVMIDEDMTARISMADVKFSFQSPGRMYAPAWVAPEAL
QKKPEDTNRRSADMWSFAVLLWELVTREVPFADLSNMEIGMKVALEGLRPTIPPGISPHV
SKLMKICMNEDPAKRPKFDMIVPILEKMQDK

Sequence of entity 2 (B), FASTA

>3KMW_2 Alpha-parvin (chains B)
GSHMDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLL
EGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYN
LFTKYRNVE

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
MG	Magnesium ion	Mg	1

Primary citation

The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions. Fukuda, K., Gupta, S., Chen, K. et al. Mol Cell (2009) 36:819-830. DOI 10.1016/j.molcel.2009.11.028 · 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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