4U5J

C-Src in complex with Ruxolitinib

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	10
Details	binding site for residue RXT A 601

Chain	Residue
A	GLY276
A	HOH780
A	VAL281
A	ALA293
A	GLU339
A	MET341
A	ALA390
A	ASN391
A	LEU393
A	ASP404

---

site_id	AC2
Number of Residues	8
Details	binding site for residue RXT B 601

Chain	Residue
B	ALA293
B	LYS295
B	GLU339
B	TYR340
B	MET341
B	GLY344
B	ALA390
B	LEU393

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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

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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

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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	ASP386
B	ASP386

---

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

Chain	Residue	Details
A	LEU273
B	LEU273

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	LYS295
B	LYS295

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:6273838, ECO:0000269|PubMed:8856081

Chain	Residue	Details
A	TYR416
B	TYR416

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:8856081

Chain	Residue	Details
A	TYR436
B	TYR436

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:19948721

Chain	Residue	Details
A	CYS498
B	CYS498

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site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by CSK => ECO:0000269|PubMed:2420005

Chain	Residue	Details
A	TYR527
B	TYR527

---