3VW8

Crystal structure of human c-Met kinase domain with its inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE DF6 A 1401

Chain	Residue
A	ILE1084
A	TYR1159
A	MET1160
A	GLY1163
A	HIS1202
A	MET1211
A	ALA1221
A	ASP1222
A	PHE1223
A	ALA1108
A	LYS1110
A	GLU1127
A	ILE1130
A	MET1131
A	LEU1140
A	LEU1157
A	PRO1158

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 1402

Chain	Residue
A	LYS1179
A	PHE1344
A	GLY1346
A	GLU1347
A	HIS1348

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Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	27
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK

Chain	Residue	Details
A	ILE1084-LYS1110

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site_id	PS00109
Number of Residues	13
Details	PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML

Chain	Residue	Details
A	PHE1200-LEU1212

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	LEU1205

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	GLY1085

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	SER1111

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12475979

Chain	Residue	Details
A	ASP1231

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979

Chain	Residue	Details
A	TYR1235

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790

Chain	Residue	Details
A	SER1236

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	PHE1290

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:7513258

Chain	Residue	Details
A	VAL1350

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