3DKC: MET receptor tyrosine kinase

Structure of MET receptor tyrosine kinase in complex with ATP. Determined by X-ray diffraction at 1.52 Å resolution. Released 7 Jul 2009.

Method: X-ray diffraction
Resolution: 1.52 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,851
Mol. weight: 36.32 kDa
Ligands: ATP, MG
Released: 7 Jul 2009

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

Secondary structure: helices and β-sheets

3DKC contains 18 α-helices and 16 β-strands across 1 chain. 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: 18 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	1055-1057	3
α-helix	1060-1065	6
β-strand	1070	1	1
β-strand	1076-1086	11	1
β-strand	1090-1098	9	1
β-strand	1104-1112	9	1
α-helix	1118-1132	15
β-strand	1139	1	2
β-strand	1144-1146	3	1
β-strand	1154-1158	5	1
β-strand	1164	1	2
α-helix	1165-1170	6
β-strand	1177	1	3
α-helix	1178-1197	20
α-helix	1207-1209	3
β-strand	1210-1212	3	2
β-strand	1218-1220	3	2
α-helix	1227-1234	8
α-helix	1237-1239	3
α-helix	1247-1249	3
α-helix	1252-1257	6
α-helix	1262-1277	16
α-helix	1281-1282	2
α-helix	1292-1297	6
α-helix	1302-1304	3
β-strand	1305	1	4
α-helix	1310-1319	10
α-helix	1324-1326	3
α-helix	1328-1329	2
α-helix	1330-1342	13
β-strand	1349	1	3
β-strand	1353	1	5
β-strand	1356	1	5
β-strand	1359	1	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Hepatocyte growth factor receptor	A	protein	317	Homo sapiens	P08581 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3DKC_1 Hepatocyte growth factor receptor (chains A)
GSLNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKI
HCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDL
RNFIRNETHNPTVKDLIGFGLQVAKGMKFLASKKFVHRDLAARNCMLDEKFTVKVADFGL
ARDMYDKEFDSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYP
DVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFI
GEHYVHVNATYVNVKEG

Ligands and cofactors

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

Water and common crystallization additives (CL) are not listed.

Primary citation

SGX523 is an exquisitely selective, ATP-competitive inhibitor of the MET receptor tyrosine kinase with antitumor activity in vivo. Buchanan, S.G., Hendle, J., Lee, P.S. et al. Mol Cancer Ther (2009) 8:3181-3190. DOI 10.1158/1535-7163.MCT-09-0477 · PubMed

Other PDB entries of the same protein (UniProt P08581 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9T6K 1.13 Å, Crystal structure of wild-type c-MET bound by glumetinib.
9T0D 1.2 Å, Crystal structure of wild-type c-MET bound by glesatinib
4R1V 1.2 Å, Identification and optimization of pyridazinones as potent and selective c-Met kinase…
9SXJ 1.31 Å, Crystal structure of wild-type c-MET bound by capmatinib.
3BUX 1.35 Å, Crystal structure of c-Cbl-TKB domain complexed with its binding motif in c-Met
3F66 1.4 Å, Human c-Met Kinase in complex with quinoxaline inhibitor
3ZCL 1.4 Å, X-ray Structure of c-Met kinase in complex with inhibitor…
9T08 1.46 Å, Crystal structure of wild-type c-MET bound by sitravatinib.
9T0B 1.54 Å, Crystal structure of D1228V c-MET bound by sitravatinib.
9C1R 1.59 Å, Crystal structure of mutant cMET D1228N kinase domain in complex with inhibitor compound…
3Q6U 1.6 Å, Structure of the apo MET receptor kinase in the dually-phosphorylated, activated state
9T3Q 1.63 Å, Crystal structure of D1228V c-MET bound by cabozantinib.

Browse structure collections

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