4ZLZ

Crystal Structure of Bruton's Tyrosine Kinase in complex with a substituted Cinnoline

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	8
Details	binding site for residue IMD A 701

Chain	Residue
A	ARG562
A	MET596
A	GLU599
A	PHE601
A	SER649
A	LEU652
A	ASP653
A	ASP656

---

site_id	AC2
Number of Residues	3
Details	binding site for residue IPA A 702

Chain	Residue
A	GLN424
A	ASP426
A	LYS420

---

site_id	AC3
Number of Residues	1
Details	binding site for residue IMD A 703

Chain	Residue
A	TRP421

---

site_id	AC4
Number of Residues	5
Details	binding site for residue DMS A 704

Chain	Residue
A	THR403
A	PHE404
A	THR628
A	TYR631
A	HOH801

---

site_id	AC5
Number of Residues	13
Details	binding site for residue 4RV A 705

Chain	Residue
A	LEU408
A	THR410
A	VAL416
A	ALA428
A	THR474
A	GLU475
A	MET477
A	ARG525
A	LEU528
A	SER538
A	ASP539
A	HOH852
A	HOH954

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU408-LYS430

---

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

Chain	Residue	Details
A	PHE517-VAL529

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
Number of Residues	7
Details	Motif: {"description":"CAV1-binding"}

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"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20052711","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3K54","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3OCT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21280133","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3PIY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by LYN and SYK","evidences":[{"source":"PubMed","id":"8630736","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9012831","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15375214","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15375214","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---