5EBZ

Crystal structure of human IKK1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
E	0004672	molecular_function	protein kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation
I	0004672	molecular_function	protein kinase activity
I	0005524	molecular_function	ATP binding
I	0006468	biological_process	protein phosphorylation
J	0004672	molecular_function	protein kinase activity
J	0005524	molecular_function	ATP binding
J	0006468	biological_process	protein phosphorylation
K	0004672	molecular_function	protein kinase activity
K	0005524	molecular_function	ATP binding
K	0006468	biological_process	protein phosphorylation
L	0004672	molecular_function	protein kinase activity
L	0005524	molecular_function	ATP binding
L	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGGFGNVClYqhreldlk..........IAIK

Chain	Residue	Details
A	LEU21-LYS44

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site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNIVL

Chain	Residue	Details
A	ILE140-LEU152

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP144
J	ASP144
K	ASP144
L	ASP144
B	ASP144
C	ASP144
D	ASP144
E	ASP144
F	ASP144
G	ASP144
H	ASP144
I	ASP144

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU21
E	LYS44
F	LEU21
F	LYS44
G	LEU21
G	LYS44
H	LEU21
H	LYS44
I	LEU21
I	LYS44
J	LEU21
A	LYS44
J	LYS44
K	LEU21
K	LYS44
L	LEU21
L	LYS44
B	LEU21
B	LYS44
C	LEU21
C	LYS44
D	LEU21
D	LYS44
E	LEU21

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	MOD_RES: Phosphothreonine; by PKB/AKT1 and SGK1 => ECO:0000269|PubMed:10485710, ECO:0000269|PubMed:19088076

Chain	Residue	Details
A	THR23
J	THR23
K	THR23
L	THR23
B	THR23
C	THR23
D	THR23
E	THR23
F	THR23
G	THR23
H	THR23
I	THR23

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: Phosphoserine; by MAP3K14 => ECO:0000269|PubMed:9520446

Chain	Residue	Details
A	GLU176
J	GLU176
K	GLU176
L	GLU176
B	GLU176
C	GLU176
D	GLU176
E	GLU176
F	GLU176
G	GLU176
H	GLU176
I	GLU176

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: (Microbial infection) O-acetylthreonine; by Yersinia YopJ => ECO:0000269|PubMed:17116858

Chain	Residue	Details
A	THR179
J	THR179
K	THR179
L	THR179
B	THR179
C	THR179
D	THR179
E	THR179
F	THR179
G	THR179
H	THR179
I	THR179

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	MOD_RES: Phosphoserine; by SGK1 => ECO:0000269|PubMed:19088076

Chain	Residue	Details
A	GLU180
J	GLU180
K	GLU180
L	GLU180
B	GLU180
C	GLU180
D	GLU180
E	GLU180
F	GLU180
G	GLU180
H	GLU180
I	GLU180

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