Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KCF

Crystal structure of TGFbRI complexed with a pyrazolone 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	15
Details	BINDING SITE FOR RESIDUE JZO A 1

Chain	Residue
A	ILE211
A	TYR282
A	HIS283
A	LYS337
A	ASN338
A	LEU340
A	ASP351
A	ALA230
A	LYS232
A	GLU245
A	LEU260
A	PHE262
A	LEU278
A	SER280
A	ASP281

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE JZO B 2

Chain	Residue
B	ALA230
B	LYS232
B	GLU245
B	TYR249
B	LEU260
B	PHE262
B	SER280
B	ASP281
B	TYR282
B	HIS283
B	LYS337
B	ASN338
B	LEU340

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE JZO C 3

Chain	Residue
C	ILE211
C	ALA230
C	LYS232
C	TYR249
C	LEU260
C	PHE262
C	LEU278
C	SER280
C	TYR282
C	HIS283
C	LYS337
C	ASN338
C	LEU340
C	ASP351

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE JZO D 4

Chain	Residue
D	ILE211
D	ALA230
D	LYS232
D	GLU245
D	TYR249
D	LEU260
D	PHE262
D	LEU278
D	SER280
D	ASP281
D	TYR282
D	HIS283
D	LYS337
D	ASN338
D	LEU340
D	ASP351

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE JZO E 5

Chain	Residue
E	ILE211
E	ALA230
E	LYS232
E	GLU245
E	TYR249
E	LEU260
E	PHE262
E	SER280
E	TYR282
E	HIS283
E	LYS337
E	ASN338
E	LEU340
E	ASP351

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 E 1

Chain	Residue
E	HIS283
E	LYS342
E	LYS343

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 6

Chain	Residue
B	HIS283
B	LYS342
B	LYS343

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 A 9

Chain	Residue
A	HIS283
A	LYS342
A	LYS343

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 C 10

Chain	Residue
C	HIS283
C	LYS342
C	LYS343

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 D 13

Chain	Residue
D	HIS283
D	LYS342
D	LYS343

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 B 12

Chain	Residue
B	PO411
B	LYS335
B	LYS337
B	THR375
B	TYR378
B	LEU426

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 2

Chain	Residue
E	PO43
E	LYS335
E	LYS337
E	THR375

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 E 3

Chain	Residue
E	ASP435
E	PO42
E	ARG377

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 B 11

Chain	Residue
B	PO412
B	ARG377
B	ASP435

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 D 15

Chain	Residue
D	PO414
D	ARG377
D	ASP435
D	PRO436

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 22

Chain	Residue
A	PO421
A	ARG377
A	ASP435
A	PRO436

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 D 14

Chain	Residue
D	PO415
D	LYS335
D	LYS337
D	THR375
D	ARG377

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 21

Chain	Residue
A	PO422
A	LYS335
A	LYS337
A	THR375

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
C	LYS232
D	ILE211
D	LYS232
E	ILE211
E	LYS232
A	ILE211
A	LYS232
B	ILE211
B	LYS232
C	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
C	THR186
D	THR185
D	THR186
E	THR185
E	THR186
A	THR185
A	THR186
B	THR185
B	THR186
C	THR185

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

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

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)