4PV0

Crystal structure of spleen tyrosine kinase (Syk) in complex with an imidazopyrazine 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	13
Details	BINDING SITE FOR RESIDUE CG4 A 701

Chain	Residue
A	LEU377
A	LYS458
A	LEU501
A	HOH835
A	HOH858
A	ALA400
A	GLU449
A	MET450
A	ALA451
A	GLU452
A	GLY454
A	PRO455
A	ASN457

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 702

Chain	Residue
A	ARG493

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 704

Chain	Residue
A	VAL536
A	LYS537

---

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 705

Chain	Residue
A	TYR631

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 706

Chain	Residue
A	GLN391
A	CYS593

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	26
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK

Chain	Residue	Details
A	LEU377-LYS402

---

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

Chain	Residue	Details
A	PHE490-LEU502

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P48025","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18369315","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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