6OKO

Crystal structure of mRIPK3 complexed with N-(3-fluoro-4-{1H-pyrrolo[2,3-b]pyridin-4-yloxy}phenyl)-1-(4-fluorophenyl)-2-oxo-1,2-dihydropyridine-3-carboxamide

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	16
Details	binding site for residue 1FN A 4000

Chain	Residue
A	VAL36
A	LEU132
A	HIS141
A	LEU150
A	LEU159
A	ALA160
A	ASP161
A	PHE162
A	ALA49
A	LYS51
A	GLU61
A	MET65
A	THR95
A	ARG96
A	PHE97
A	MET98

---

site_id	AC2
Number of Residues	16
Details	binding site for residue 1FN B 4000

Chain	Residue
B	VAL36
B	ALA49
B	LYS51
B	GLU61
B	LEU68
B	THR95
B	ARG96
B	PHE97
B	MET98
B	LEU132
B	HIS141
B	LEU150
B	LEU159
B	ALA160
B	ASP161
B	PHE162

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL28-LYS51

---

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

Chain	Residue	Details
A	LEU139-LEU151

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:10490590, ECO:0000305|PubMed:24095729

Chain	Residue	Details
A	ASP143
B	ASP143

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:24095729, ECO:0007744|PDB:4M69

Chain	Residue	Details
A	VAL28
B	VAL28

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:24095729, ECO:0007744|PDB:4M69

Chain	Residue	Details
A	LYS51
B	LYS51

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:23612963

Chain	Residue	Details
A	SER2
A	SER165
A	SER304
B	SER2
B	SER165
B	SER304

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9Y572

Chain	Residue	Details
A	THR187
B	THR187

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q9Y572

Chain	Residue	Details
A	SER204
B	SER204

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23612963, ECO:0000269|PubMed:27819682

Chain	Residue	Details
A	THR231
B	THR231

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23612963, ECO:0000269|PubMed:27819682

Chain	Residue	Details
A	SER232
B	SER232

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:23612963

Chain	Residue	Details
A	THR257
B	THR257

---