5KX8

Irak4-inhibitor co-structure

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	12
Details	binding site for residue 6YE A 501

Chain	Residue
A	MET192
A	LEU318
A	SER328
A	ASP329
A	ALA211
A	TYR262
A	VAL263
A	MET265
A	PRO266
A	GLY268
A	ALA315
A	ASN316

---

site_id	AC2
Number of Residues	16
Details	binding site for residue 6YE B 501

Chain	Residue
B	MET192
B	GLU194
B	GLY195
B	VAL200
B	ALA211
B	TYR262
B	VAL263
B	TYR264
B	MET265
B	PRO266
B	GLY268
B	ALA315
B	ASN316
B	LEU318
B	SER328
B	ASP329

---

site_id	AC3
Number of Residues	12
Details	binding site for residue 6YE C 501

Chain	Residue
C	VAL200
C	ALA211
C	TYR262
C	VAL263
C	MET265
C	PRO266
C	GLY268
C	ALA315
C	ASN316
C	LEU318
C	SER328
C	ASP329

---

site_id	AC4
Number of Residues	16
Details	binding site for residue 6YE D 501

Chain	Residue
D	MET192
D	GLU194
D	GLY195
D	VAL200
D	ALA211
D	TYR262
D	VAL263
D	TYR264
D	MET265
D	PRO266
D	GLY268
D	ALA315
D	ASN316
D	LEU318
D	SER328
D	ASP329

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ASP311
B	ASP311
C	ASP311
D	ASP311

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	MET192
B	MET192
C	MET192
D	MET192

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING:

Chain	Residue	Details
A	LYS213
D	LYS213
D	LYS313
D	ASP329
A	LYS313
A	ASP329
B	LYS213
B	LYS313
B	ASP329
C	LYS213
C	LYS313
C	ASP329

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32

Chain	Residue	Details
A	TPO342
B	TPO342
C	TPO342
D	TPO342

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:17161373, ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32

Chain	Residue	Details
A	TPO345
B	TPO345
C	TPO345
D	TPO345

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:17161373, ECO:0000269|PubMed:17312103

Chain	Residue	Details
A	SEP346
B	SEP346
C	SEP346
D	SEP346

---