5AR3

RIP2 Kinase Catalytic Domain (1 - 310) complex with AMP-PCP

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ACP A 1311

Chain	Residue
A	LEU24
A	MET98
A	GLU105
A	GLN150
A	ASN151
A	LEU153
A	ASP164
A	MG1312
A	HOH2005
A	HOH2023
A	HOH2045
A	ALA28
A	SER29
A	GLY30
A	ALA45
A	LYS47
A	THR95
A	GLU96
A	TYR97

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ACP B 1311

Chain	Residue
B	SER25
B	GLY27
B	ALA28
B	SER29
B	GLY30
B	ALA45
B	LYS47
B	THR95
B	GLU96
B	MET98
B	GLU105
B	ASN151
B	LEU153
B	ASP164
B	MG1312
B	HOH2008

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 1312

Chain	Residue
A	ASN151
A	ASP164
A	ACP1311
A	HOH2023

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 1312

Chain	Residue
B	ASN151
B	ASP164
B	ACP1311

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU142-LEU154

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:9705938

Chain	Residue	Details
A	ASP146
B	ASP146

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU24
B	LEU24

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
A	LYS47
B	LYS47

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: (Microbial infection) O-acetylthreonine; by Yersinia YopJ => ECO:0000269|PubMed:22520462

Chain	Residue	Details
A	THR149
A	THR189
B	THR149
B	THR189

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195

Chain	Residue	Details
A	SER168
B	SER168

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Phosphoserine; alternate => ECO:0000269|PubMed:28545134

Chain	Residue	Details
A	SER174
A	SER178
A	SER181
B	SER174
B	SER178
B	SER181

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis and LRRK2; alternate => ECO:0000269|PubMed:16824733, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28545134

Chain	Residue	Details
A	SER176
B	SER176

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:28545134

Chain	Residue	Details
A	SER180
B	SER180

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: (Microbial infection) O-acetylserine; by Yersinia YopJ => ECO:0000269|PubMed:22520462

Chain	Residue	Details
A	SER183
B	SER183

---

site_id	SWS_FT_FI10
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18079694

Chain	Residue	Details
A	LYS209
B	LYS209

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