4NEU

X-ray structure of Receptor Interacting Protein 1 (RIP1)kinase domain with a 1-aminoisoquinoline inhibitor

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	5
Details	BINDING SITE FOR RESIDUE MG A 401

Chain	Residue
A	SER14
A	SER14
A	PHE17
A	PHE17
A	LEU18

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site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE Q1A A 402

Chain	Residue
A	VAL76
A	MET92
A	GLU93
A	TYR94
A	MET95
A	LEU145
A	ALA155
A	ASP156
A	LEU157
A	ILE43
A	GLU63
A	MET67
A	LEU70

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE Q1A B 401

Chain	Residue
B	ILE43
B	GLU63
B	MET66
B	MET67
B	LEU70
B	VAL75
B	VAL76
B	MET92
B	GLU93
B	TYR94
B	MET95
B	LEU145
B	ALA155
B	ASP156

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL134-VAL146

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP138
B	ASP138

---

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

Chain	Residue	Details
A	LEU23
A	LYS45
B	LEU23
B	LYS45

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Cleavage; by CASP8 => ECO:0000269|PubMed:10521396, ECO:0000269|PubMed:31827280, ECO:0000269|PubMed:31827281

Chain	Residue	Details
A	ASP324
B	ASP324

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine; by IKKA and IKKB => ECO:0000269|PubMed:18408713

Chain	Residue	Details
A	SER6
B	SER6

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255

Chain	Residue	Details
A	SER20
B	SER20

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine; by IKKA and IKKB => ECO:0000269|PubMed:18408713, ECO:0000269|PubMed:30988283

Chain	Residue	Details
A	SER25
B	SER25

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine; by RIPK3 and autocatalysis => ECO:0000255

Chain	Residue	Details
A	SER161
B	SER161

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255, ECO:0000269|PubMed:29440439, ECO:0000269|PubMed:31827280

Chain	Residue	Details
A	SER166
B	SER166

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:18408713

Chain	Residue	Details
A	SER303
B	SER303

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphoserine; by MAP3K7 => ECO:0000269|PubMed:18408713, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER320
B	SER320

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