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6FU5

Structure of the kinase domain of human RIPK2 in complex with the inhibitor CSLP18

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue E7N A 400
ChainResidue
ALEU24
AMET98
AGLU105
AGLN150
ALEU153
AALA163
AASP164
ASER25
ASER29
AVAL32
AALA45
ALYS47
AGLU66
ATHR95
AGLU96

site_idAC2
Number of Residues14
Detailsbinding site for residue E7N B 400
ChainResidue
BLEU24
BSER25
BVAL32
BALA45
BLYS47
BGLU66
BTHR95
BGLU96
BMET98
BGLU105
BGLN150
BASN151
BLEU153
BASP164

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LlHhDLKtqNILL
ChainResidueDetails
ALEU142-LEU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:9705938
ChainResidueDetails
AASP146
BASP146

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU24
BLEU24

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS47
BLYS47

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: (Microbial infection) O-acetylthreonine; by Yersinia YopJ => ECO:0000269|PubMed:22520462
ChainResidueDetails
ATHR149
ATHR189
BTHR149
BTHR189

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER168
BSER168

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Phosphoserine; alternate => ECO:0000269|PubMed:28545134
ChainResidueDetails
ASER174
ASER178
ASER181
BSER174
BSER178
BSER181

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis and LRRK2; alternate => ECO:0000269|PubMed:16824733, ECO:0000269|PubMed:27830463, ECO:0000269|PubMed:28545134
ChainResidueDetails
ASER176
BSER176

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:28545134
ChainResidueDetails
ASER180
BSER180

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: (Microbial infection) O-acetylserine; by Yersinia YopJ => ECO:0000269|PubMed:22520462
ChainResidueDetails
ASER183
BSER183

site_idSWS_FT_FI10
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:18079694
ChainResidueDetails
ALYS209
BLYS209

229183

PDB entries from 2024-12-18

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