6VQL

CRYSTAL STRUCTURE OF INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE 4 (IRAK4-WT) COMPLEX WITH A NICOTINAMIDE INHIBITOR

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
C	0000287	molecular_function	magnesium ion binding
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
C	0007165	biological_process	signal transduction
D	0000287	molecular_function	magnesium ion binding
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
D	0007165	biological_process	signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue R7S A 501

Chain	Residue
A	ILE185
A	PRO266
A	ASN267
A	GLY268
A	ARG273
A	LEU318
A	SER328
A	MET192
A	VAL200
A	ALA211
A	VAL246
A	TYR262
A	VAL263
A	TYR264
A	MET265

---

site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 A 502

Chain	Residue
A	GLY350
A	THR352

---

site_id	AC3
Number of Residues	14
Details	binding site for residue R7S B 501

Chain	Residue
B	MET192
B	ALA211
B	VAL246
B	TYR262
B	VAL263
B	TYR264
B	MET265
B	PRO266
B	ASN267
B	GLY268
B	ARG273
B	LEU318
B	SER328
B	HOH604

---

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 B 502

Chain	Residue
B	ILE403
B	GLU404
B	TYR430
B	SER434

---

site_id	AC5
Number of Residues	2
Details	binding site for residue SO4 B 503

Chain	Residue
B	HIS166
B	SER167

---

site_id	AC6
Number of Residues	4
Details	binding site for residue SO4 B 504

Chain	Residue
B	LYS400
B	HIS438
B	GLU439
D	LYS440

---

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 B 505

Chain	Residue
B	GLY350
B	THR351
B	THR352

---

site_id	AC8
Number of Residues	15
Details	binding site for residue R7S C 501

Chain	Residue
C	MET192
C	ALA211
C	VAL246
C	TYR262
C	VAL263
C	TYR264
C	MET265
C	PRO266
C	GLY268
C	ARG273
C	THR280
C	LEU318
C	SER328
C	HOH602
C	HOH603

---

site_id	AC9
Number of Residues	2
Details	binding site for residue SO4 C 502

Chain	Residue
A	ASN207
C	SER423

---

site_id	AD1
Number of Residues	3
Details	binding site for residue SO4 C 503

Chain	Residue
C	HIS438
C	GLU439
C	LYS440

---

site_id	AD2
Number of Residues	2
Details	binding site for residue SO4 C 504

Chain	Residue
A	HIS166
C	THR458

---

site_id	AD3
Number of Residues	15
Details	binding site for residue R7S D 501

Chain	Residue
D	MET192
D	VAL200
D	ALA211
D	VAL246
D	TYR262
D	VAL263
D	TYR264
D	MET265
D	PRO266
D	ASN267
D	GLY268
D	ARG273
D	LEU318
D	SER328
D	HOH610

---

site_id	AD4
Number of Residues	2
Details	binding site for residue SO4 D 502

Chain	Residue
B	ASN207
D	SER423

---

site_id	AD5
Number of Residues	5
Details	binding site for residue SO4 D 503

Chain	Residue
C	HIS166
C	SER167
D	PHE165
D	HIS166
D	SER167

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
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	32
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
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_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17161373","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
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

---