2X7O

Crystal structure of TGFbRI complexed with an indolinone inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
A	0016020	cellular_component	membrane
B	0004672	molecular_function	protein kinase activity
B	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
B	0016020	cellular_component	membrane
C	0004672	molecular_function	protein kinase activity
C	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
C	0016020	cellular_component	membrane
D	0004672	molecular_function	protein kinase activity
D	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
D	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
D	0016020	cellular_component	membrane
E	0004672	molecular_function	protein kinase activity
E	0004675	molecular_function	transmembrane receptor protein serine/threonine kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
E	0007178	biological_process	cell surface receptor protein serine/threonine kinase signaling pathway
E	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ZOP A 600

Chain	Residue
A	ILE211
A	ASP281
A	HIS283
A	GLU284
A	HIS285
A	GLY286
A	ASP290
A	ARG294
A	LEU340
A	GLY212
A	VAL219
A	ALA230
A	LYS232
A	GLU245
A	LEU260
A	LEU278
A	SER280

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ZOP B 600

Chain	Residue
B	ILE211
B	VAL219
B	ALA230
B	LYS232
B	GLU245
B	LEU260
B	LEU278
B	SER280
B	ASP281
B	TYR282
B	HIS283
B	GLU284
B	GLY286
B	ASP290
B	ARG294
B	LEU340

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ZOP C 600

Chain	Residue
C	ILE211
C	GLY212
C	VAL219
C	ALA230
C	LYS232
C	GLU245
C	LEU260
C	LEU278
C	SER280
C	ASP281
C	TYR282
C	HIS283
C	GLU284
C	HIS285
C	GLY286
C	ASP290
C	ARG294
C	LEU340
C	ASP351

---

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ZOP D 600

Chain	Residue
D	ILE211
D	GLY212
D	VAL219
D	ALA230
D	LYS232
D	GLU245
D	LEU260
D	LEU278
D	SER280
D	ASP281
D	TYR282
D	HIS283
D	GLU284
D	HIS285
D	GLY286
D	ASP290
D	LEU340
D	ASP351

---

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ZOP E 600

Chain	Residue
E	ILE211
E	GLY212
E	VAL219
E	ALA230
E	LYS232
E	GLU245
E	LEU260
E	LEU278
E	SER280
E	ASP281
E	TYR282
E	HIS283
E	GLU284
E	HIS285
E	GLY286
E	ASP290
E	ARG294
E	LEU340

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	22
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGRFGEVWrGkwrgee............VAVK

Chain	Residue	Details
A	ILE211-LYS232

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHrDLKskNILV

Chain	Residue	Details
A	ILE329-VAL341

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP333
B	ASP333
C	ASP333
D	ASP333
E	ASP333

---

site_id	SWS_FT_FI2
Number of Residues	10
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE211
E	LYS232
A	LYS232
B	ILE211
B	LYS232
C	ILE211
C	LYS232
D	ILE211
D	LYS232
E	ILE211

---

site_id	SWS_FT_FI3
Number of Residues	5
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER165
B	SER165
C	SER165
D	SER165
E	SER165

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	MOD_RES: Phosphothreonine; by TGFBR2 => ECO:0000269|PubMed:7774578

Chain	Residue	Details
A	THR185
E	THR186
A	THR186
B	THR185
B	THR186
C	THR185
C	THR186
D	THR185
D	THR186
E	THR185

---

site_id	SWS_FT_FI5
Number of Residues	15
Details	MOD_RES: Phosphoserine; by TGFBR2 => ECO:0000269|PubMed:7774578

Chain	Residue	Details
A	SER187
D	SER187
D	SER189
D	SER191
E	SER187
E	SER189
E	SER191
A	SER189
A	SER191
B	SER187
B	SER189
B	SER191
C	SER187
C	SER189
C	SER191

---

site_id	SWS_FT_FI6
Number of Residues	10
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) => ECO:0000250

Chain	Residue	Details
A	LYS391
B	LYS391
C	LYS391
D	LYS391
E	LYS391

---