4U9A

Sulphur Anomalous Crystal Structure of Asymmetric IRAK4 Dimer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
A	0007165	biological_process	signal transduction
B	0000287	molecular_function	magnesium ion binding
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
B	0007165	biological_process	signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue STU A 501

Chain	Residue
A	MET192
A	MET265
A	ALA315
A	ASN316
A	LEU318
A	SER328
B	SO4502
A	GLY193
A	GLU194
A	GLY195
A	VAL200
A	ALA211
A	LYS213
A	VAL263
A	TYR264

---

site_id	AC2
Number of Residues	15
Details	binding site for residue STU B 501

Chain	Residue
B	MET192
B	GLY193
B	GLU194
B	VAL200
B	ALA211
B	TYR262
B	VAL263
B	TYR264
B	MET265
B	GLY268
B	ALA315
B	ASN316
B	LEU318
B	SER328
B	SO4503

---

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 B 502

Chain	Residue
A	GLY195
A	LYS313
A	STU501
B	THR345

---

site_id	AC4
Number of Residues	1
Details	binding site for residue SO4 B 503

Chain	Residue
B	STU501

---

site_id	AC5
Number of Residues	3
Details	binding site for residue SO4 B 504

Chain	Residue
B	THR365
B	LYS367
B	LYS441

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2006","submissionDatabase":"PDB data bank","title":"Crystal structures of the apo and inhibited IRAK4 kinase domain.","authors":["Mol C.D.","Arduini R.M.","Baker D.P.","Chien E.Y.","Dougan D.R.","Friedman J.","Gibaja V.","Hession C.A.","Horne A."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17161373","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2006","submissionDatabase":"PDB data bank","title":"Crystal structures of the apo and inhibited IRAK4 kinase domain.","authors":["Mol C.D.","Arduini R.M.","Baker D.P.","Chien E.Y.","Dougan D.R.","Friedman J.","Gibaja V.","Hession C.A.","Horne A."]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17161373","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---