Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6E6E

DGY-06-116, a novel and selective covalent inhibitor of SRC kinase

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
C	0004672	molecular_function	protein kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004713	molecular_function	protein tyrosine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
E	0004672	molecular_function	protein kinase activity
E	0004713	molecular_function	protein tyrosine kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0004713	molecular_function	protein tyrosine kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0004713	molecular_function	protein tyrosine kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0004713	molecular_function	protein tyrosine kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue HVY A 601

Chain	Residue
A	LEU276
A	TYR343
A	MET344
A	GLY347
A	ASN394
A	LEU396
A	ALA406
A	HOH701
A	GLY279
A	CYS280
A	VAL284
A	ALA296
A	LYS298
A	VAL326
A	ILE339
A	THR341

site_id	AC2
Number of Residues	19
Details	binding site for Di-peptide HVY B 601 and CYS B 277

Chain	Residue
B	LEU276
B	GLY279
B	PHE281
B	GLY282
B	VAL284
B	ALA296
B	LYS298
B	GLU313
B	VAL326
B	ILE339
B	THR341
B	TYR343
B	MET344
B	SER345
B	GLY347
B	ASN394
B	LEU396
B	ALA406
B	HOH709

site_id	AC3
Number of Residues	17
Details	binding site for Di-peptide HVY C 601 and CYS C 277

Chain	Residue
C	LEU276
C	GLY279
C	PHE281
C	GLY282
C	VAL284
C	ALA296
C	LYS298
C	VAL326
C	ILE339
C	THR341
C	MET344
C	GLY347
C	ASN394
C	LEU396
C	ALA406
C	ASP407
C	HOH722

site_id	AC4
Number of Residues	17
Details	binding site for Di-peptide HVY D 601 and CYS D 277

Chain	Residue
D	LEU276
D	GLY279
D	PHE281
D	GLY282
D	VAL284
D	ALA296
D	LYS298
D	GLU313
D	VAL326
D	ILE339
D	THR341
D	MET344
D	GLY347
D	ASN394
D	LEU396
D	ALA406
D	ASP407

site_id	AC5
Number of Residues	17
Details	binding site for Di-peptide HVY E 601 and CYS E 277

Chain	Residue
E	GLY279
E	PHE281
E	VAL284
E	ALA296
E	LYS298
E	GLU313
E	VAL326
E	ILE339
E	THR341
E	TYR343
E	MET344
E	GLY347
E	ASN394
E	LEU396
E	ALA406
E	ASP407
E	HOH711

site_id	AC6
Number of Residues	17
Details	binding site for Di-peptide HVY F 601 and CYS F 277

Chain	Residue
F	LEU396
F	ALA406
F	ASP407
F	HOH711
F	GLY279
F	PHE281
F	GLY282
F	VAL284
F	ALA296
F	LYS298
F	GLU313
F	VAL326
F	ILE339
F	THR341
F	TYR343
F	MET344
F	GLY347

site_id	AC7
Number of Residues	17
Details	binding site for Di-peptide HVY G 601 and CYS G 277

Chain	Residue
G	LEU276
G	GLY279
G	PHE281
G	VAL284
G	ALA296
G	LYS298
G	GLU313
G	VAL326
G	THR341
G	TYR343
G	MET344
G	GLY347
G	ASN394
G	LEU396
G	ALA406
G	ASP407
G	HOH704

site_id	AC8
Number of Residues	15
Details	binding site for Di-peptide HVY H 601 and CYS H 277

Chain	Residue
H	LEU276
H	GLY279
H	PHE281
H	GLY282
H	VAL284
H	ALA296
H	LYS298
H	VAL326
H	THR341
H	MET344
H	GLY347
H	ASN394
H	LEU396
H	ALA406
H	HOH706

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	23
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGCFGEVWmGtwngttr...........VAIK

Chain	Residue	Details
A	LEU276-LYS298

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

Chain	Residue	Details
A	TYR385-VAL397

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP389
B	ASP389
C	ASP389
D	ASP389
E	ASP389
F	ASP389
G	ASP389
H	ASP389

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING:

Chain	Residue	Details
E	LEU276
E	LYS298
F	LEU276
F	LYS298
G	LEU276
G	LYS298
H	LEU276
H	LYS298
A	LEU276
A	LYS298
B	LEU276
B	LYS298
C	LEU276
C	LYS298
D	LEU276
D	LYS298

site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Phosphotyrosine; by FAK2 => ECO:0000250

Chain	Residue	Details
E	TYR419
F	TYR419
G	TYR419
H	TYR419
A	TYR419
B	TYR419
C	TYR419
D	TYR419

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphotyrosine; by CSK => ECO:0000269\|PubMed:19307596, ECO:0000269\|PubMed:26936507, ECO:0000269\|PubMed:7525268, ECO:0000269\|PubMed:7929427, ECO:0007744\|PubMed:19369195

Chain	Residue	Details
E	TYR530
F	TYR530
G	TYR530
H	TYR530
A	TYR530
B	TYR530
C	TYR530
D	TYR530

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