3IEC

Helicobacter pylori CagA Inhibits PAR1/MARK Family Kinases by Mimicking Host Substrates

Functional Information from GO Data

Chain	GOid	namespace	contents
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
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
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
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

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE59-LYS82

---

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

Chain	Residue	Details
A	ILE171-LEU183

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9H0K1, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP175
B	ASP175
C	ASP175
D	ASP175

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9H0K1, ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	ILE59
B	ILE59
C	ILE59
D	ILE59

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:O08678, ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LYS82
B	LYS82
C	LYS82
D	LYS82

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:O08679

Chain	Residue	Details
A	THR58
A	THR275
B	THR58
B	THR275
C	THR58
C	THR275
D	THR58
D	THR275

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: Phosphoserine; by CaMK1 => ECO:0000250|UniProtKB:O08679

Chain	Residue	Details
A	SER91
D	SER91
D	SER92
D	SER93
A	SER92
A	SER93
B	SER91
B	SER92
B	SER93
C	SER91
C	SER92
C	SER93

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by LKB1 and TAOK1 => ECO:0000269|PubMed:14976552, ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	THR208
B	THR208
C	THR208
D	THR208

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine; by GSK3-beta => ECO:0000250|UniProtKB:O08679

Chain	Residue	Details
A	SER212
B	SER212
C	SER212
D	SER212

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:O08679

Chain	Residue	Details
A	SER274
B	SER274
C	SER274
D	SER274

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by CaMK1 => ECO:0000250|UniProtKB:O08679

Chain	Residue	Details
A	THR294
B	THR294
C	THR294
D	THR294

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP175
A	GLU179

---

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	SER212
B	ASP175
B	LYS177

---

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	SER212
C	ASP175
C	LYS177

---

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	SER212
D	ASP175
D	LYS177

---

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP175
A	ASN180
A	LYS177

---

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP175
B	ASN180
B	LYS177

---

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP175
C	ASN180
C	LYS177

---

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP175
D	ASN180
D	LYS177

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP175
B	GLU179

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP175
C	GLU179

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP175
D	GLU179

---

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	ASP175
A	LYS177

---

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
B	ASP175
B	LYS177

---

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
C	ASP175
C	LYS177

---

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
D	ASP175
D	LYS177

---

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1ir3

Chain	Residue	Details
A	SER212
A	ASP175
A	LYS177

---