6R5F

Crystal structure of RIP1 kinase in complex with DHP77

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue JSW A 301

Chain	Residue
A	ILE43
A	VAL134
A	HIS136
A	ILE154
A	ALA155
A	ASP156
A	LEU157
A	LEU159
A	SER161
A	PHE162
A	MET44
A	LYS45
A	MET67
A	LEU70
A	VAL76
A	LEU78
A	MET92
A	LEU129

---

site_id	AC2
Number of Residues	17
Details	binding site for residue JSW B 301

Chain	Residue
B	ILE43
B	MET44
B	LYS45
B	MET67
B	LEU70
B	VAL76
B	LEU78
B	MET92
B	LEU129
B	HIS136
B	ILE154
B	ALA155
B	ASP156
B	LEU157
B	LEU159
B	SER161
B	PHE162

---

site_id	AC3
Number of Residues	12
Details	binding site for residue JSW C 301

Chain	Residue
C	LYS45
C	MET67
C	VAL76
C	LEU90
C	MET92
C	LEU129
C	HIS136
C	ILE154
C	ALA155
C	ASP156
C	SER161
C	PHE162

---

site_id	AC4
Number of Residues	11
Details	binding site for residue JSW D 301

Chain	Residue
D	LYS45
D	MET67
D	VAL75
D	VAL76
D	LEU78
D	MET92
D	ILE154
D	ALA155
D	ASP156
D	LEU157
D	PHE162

---

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

---

Functional Information from SwissProt/UniProt

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

Chain	Residue	Details
A	ASP138
B	ASP138
C	ASP138
D	ASP138

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU23
A	LYS45
B	LEU23
B	LYS45
C	LEU23
C	LYS45
D	LEU23
D	LYS45

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine; by IKKA and IKKB => ECO:0000269|PubMed:18408713

Chain	Residue	Details
A	SER6
B	SER6
C	SER6
D	SER6

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255

Chain	Residue	Details
A	SER20
B	SER20
C	SER20
D	SER20

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine; by IKKA and IKKB => ECO:0000269|PubMed:18408713, ECO:0000269|PubMed:30988283

Chain	Residue	Details
A	SER25
B	SER25
C	SER25
D	SER25

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphoserine; by RIPK3 and autocatalysis => ECO:0000255

Chain	Residue	Details
A	SER161
B	SER161
C	SER161
D	SER161

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255, ECO:0000269|PubMed:29440439, ECO:0000269|PubMed:31827280

Chain	Residue	Details
A	SER166
B	SER166
C	SER166
D	SER166

---