5DG5

CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HEPATOCYTE GROWTH FACTOR RECEPTOR C-MET IN COMPLEX WITH ALTIRATINIB ANALOG DP-4157

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
B	0004672	molecular_function	protein kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue 5B4 A 1401

Chain	Residue
A	VAL1092
A	MET1160
A	LYS1161
A	GLY1163
A	LEU1195
A	PHE1200
A	MET1211
A	VAL1220
A	ALA1221
A	ASP1222
A	PHE1223
A	ALA1108
A	TYR1234
A	LYS1110
A	MET1131
A	VAL1139
A	LEU1140
A	LEU1157
A	PRO1158
A	TYR1159

---

site_id	AC2
Number of Residues	20
Details	binding site for residue 5B4 B 1401

Chain	Residue
B	VAL1092
B	ALA1108
B	LYS1110
B	MET1131
B	VAL1139
B	LEU1140
B	LEU1157
B	PRO1158
B	TYR1159
B	MET1160
B	LYS1161
B	GLY1163
B	LEU1195
B	PHE1200
B	MET1211
B	VAL1220
B	ALA1221
B	ASP1222
B	PHE1223
B	TYR1234

---

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	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	LEU1186
B	LEU1186

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	VAL1066
B	VAL1066

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	VAL1092
B	VAL1092

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:12475979

Chain	Residue	Details
A	LEU1212
B	LEU1212

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979

Chain	Residue	Details
A	PHE1216
B	PHE1216

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:1655790

Chain	Residue	Details
A	THR1217
B	THR1217

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	VAL1271
B	VAL1271

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:7513258

Chain	Residue	Details
A	SER1331
B	SER1331

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:15735664, ECO:0000269|PubMed:7513258

Chain	Residue	Details
A	SER1338
B	SER1338

---