6L8L

C-Src in complex with ibrutinib

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue 1E8 A 600

Chain	Residue
A	LEU273
A	ASP348
A	LEU393
A	ALA403
A	ASP404
A	PHE405
A	VAL281
A	LYS295
A	ILE336
A	THR338
A	GLU339
A	MET341
A	GLY344
A	SER345

---

site_id	AC2
Number of Residues	16
Details	binding site for residue 1E8 B 600

Chain	Residue
B	GLY274
B	VAL281
B	LYS295
B	VAL323
B	ILE336
B	THR338
B	GLU339
B	MET341
B	LYS343
B	GLY344
B	SER345
B	ASP348
B	LEU393
B	ALA403
B	ASP404
B	PHE405

---

site_id	AC3
Number of Residues	10
Details	binding site for residue 1E8 C 600

Chain	Residue
C	LEU273
C	GLY274
C	ALA293
C	ILE336
C	THR338
C	GLU339
C	SER345
C	LEU393
C	ASP404
C	PHE405

---

site_id	AC4
Number of Residues	13
Details	binding site for residue 1E8 D 600

Chain	Residue
D	VAL281
D	ALA293
D	LYS295
D	ILE336
D	THR338
D	GLU339
D	MET341
D	GLY344
D	SER345
D	ASP348
D	LEU393
D	ASP404
D	PHE405

---

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	LEU273-LYS295

---

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

Chain	Residue	Details
A	TYR382-VAL394

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028

Chain	Residue	Details
A	ASP386
B	ASP386
C	ASP386
D	ASP386

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU273
B	LEU273
C	LEU273
D	LEU273

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	LYS295
B	LYS295
C	LYS295
D	LYS295

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:8856081

Chain	Residue	Details
A	TYR416
B	TYR416
C	TYR416
D	TYR416

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8856081

Chain	Residue	Details
A	TYR436
B	TYR436
C	TYR436
D	TYR436

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:19948721

Chain	Residue	Details
A	CYS498
B	CYS498
C	CYS498
D	CYS498

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:2420005

Chain	Residue	Details
A	TYR527
B	TYR527
C	TYR527
D	TYR527

---