3A4P

human c-MET kinase domain complexed with 6-benzyloxyquinoline 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	5
Details	BINDING SITE FOR RESIDUE CL A 1

Chain	Residue
A	HOH21
A	LYS1179
A	GLY1346
A	GLU1347
A	HIS1348

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IPA A 1361

Chain	Residue
A	DFQ1362
A	ARG1208
A	ASN1209
A	TYR1230
A	ASP1231

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA A 2

Chain	Residue
A	ASP1310
A	TYR1313
A	GLU1314
A	SER1335

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DFQ A 1362

Chain	Residue
A	ILE1084
A	VAL1092
A	ALA1108
A	LEU1157
A	PRO1158
A	TYR1159
A	MET1160
A	LYS1161
A	HIS1162
A	GLY1163
A	ASN1209
A	MET1211
A	ALA1221
A	ASP1222
A	TYR1230
A	IPA1361

---

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

---

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

---

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	ASP1204

---

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

Chain	Residue	Details
A	ILE1084

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	LYS1110

---

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

Chain	Residue	Details
A	TYR1230

---

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

Chain	Residue	Details
A	PHE1234

---

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	ASP1235

---

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

Chain	Residue	Details
A	THR1289

---

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	TYR1349

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258

Chain	Residue	Details
A	TYR1356

---