3ZCL: C-Met kinase

X-ray Structure of c-Met kinase in complex with inhibitor (S)-3-(1-(1H-pyrrolo(2,3-b)pyridin-3-yl)ethyl)-N-isopropyl-(1,2,4)triazolo(4,3- b)pyridazin-6-amine. Determined by X-ray diffraction at 1.4 Å resolution. Released 27 Nov 2013.

Method: X-ray diffraction
Resolution: 1.4 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 2,670
Mol. weight: 35.2 kDa
Ligands: 5TF
Released: 27 Nov 2013

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

Secondary structure: helices and β-sheets

3ZCL contains 22 α-helices and 12 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: 22 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	1055-1057	3
α-helix	1060-1067	8
β-strand	1070	1	1
α-helix	1073-1075	3
β-strand	1076-1086	11	1
β-strand	1091-1097	7	1
β-strand	1105-1111	7	1
α-helix	1118-1128	11
α-helix	1129-1133	5
β-strand	1139	1	2
β-strand	1144-1146	3	1
α-helix	1153	1
β-strand	1154-1158	5	1
β-strand	1164	1	2
α-helix	1165-1170	6
α-helix	1178-1197	20
α-helix	1207-1209	3
β-strand	1210-1212	3	2
β-strand	1218-1220	3	2
α-helix	1224-1226	3
α-helix	1232-1234	3
β-strand	1236	1	3
β-strand	1245	1	3
α-helix	1247-1249	3
α-helix	1252-1257	6
α-helix	1262-1277	16
α-helix	1281-1282	2
α-helix	1289-1291	3
α-helix	1292-1297	6
α-helix	1302-1305	4
α-helix	1310-1319	10
α-helix	1324-1326	3
α-helix	1328-1329	2
α-helix	1330-1342	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Hepatocyte growth factor receptor	A	protein	306	HOMO SAPIENS	P08581 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3ZCL_1 HEPATOCYTE GROWTH FACTOR RECEPTOR (chains A)
MVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDGKKIHCAV
KSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFI
RNETHNPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDEKFTVKVADFGLARDM
YDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNT
FDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFSELVSRISAIFSTFIGEHH
HHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
5TF	(S)-3-(1-(1H-pyrrolo(2,3-b)pyridin-3-yl)ethyl)-N-isopropyl-(1,2,4)triazolo(4,3-…	C17 H19 N7	1

Primary citation

Lessons from (S)-6-(1-(6-(1-Methyl-1H-Pyrazol-4-Yl)-[1,2, 4]Triazolo[4,3-B]Pyridazin-3-Yl)Ethyl)Quinoline (Pf-04254644), an Inhibitor of Receptor Tyrosine Kinase C-met with High Protein Kinase Selectivity But Broad Phosphodiesterase Family Inhibition Leading to Myocardial Degeneration in Rats. Cui, J.J., Shen, H., Tran-Dube, M. et al. J Med Chem (2013) 56:6651. DOI 10.1021/JM400926X · 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
9T08 1.46 Å, Crystal structure of wild-type c-MET bound by sitravatinib.
3DKC 1.52 Å, Structure of MET receptor tyrosine kinase in complex with ATP
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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