1Y57

Structure of unphosphorylated c-Src in complex with an inhibitor

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 535

Chain	Residue
A	ARG155
A	ARG175
A	SER177
A	GLU178
A	THR179
A	HOH910

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 536

Chain	Residue
A	ARG155
A	ARG156
A	LYS356

---

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 537

Chain	Residue
A	TYR340
A	MET341
A	SER342
A	GLY395
A	GLU396
A	HOH635
A	HOH755
A	HOH815

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 538

Chain	Residue
A	LYS203
A	ARG205

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 539

Chain	Residue
A	ARG388
A	ALA390
A	ASN391
A	MPZ600
A	HOH666

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MPZ A 600

Chain	Residue
A	LEU273
A	GLN275
A	VAL281
A	ALA293
A	GLU339
A	TYR340
A	MET341
A	GLY344
A	LEU393
A	SO4539
A	HOH732
A	HOH742

---

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	97
Details	Domain: {"description":"SH2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00191","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	253
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	9
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P05480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by FAK2","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by CSK","evidences":[{"source":"PubMed","id":"19307596","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26936507","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7525268","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7929427","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP386
A	ALA390

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ARG388
A	ASP386

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ARG388
A	ASN391
A	ASP386

---