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4M69

Crystal structure of the mouse RIP3-MLKL complex

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 Residues28
DetailsBINDING SITE FOR RESIDUE ANP A 401
ChainResidue
AVAL28
ALYS51
ATHR95
AARG96
APHE97
AMET98
ASER102
AASP143
ALYS145
ASER147
AASN148
AGLY29
ALEU150
AASP161
AMG403
AHOH526
AHOH551
AHOH574
AHOH583
AHOH584
AHOH594
ALYS30
AGLY31
AGLY32
APHE33
AGLY34
AVAL36
AALA49

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG69
AASN70
AGLU71
AVAL73
ALEU75
AARG96
ALYS158
AHOH528

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 403
ChainResidue
AASN148
AASP161
AANP401
AHOH593

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 404
ChainResidue
AASP86

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 405
ChainResidue
AARG42

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 501
ChainResidue
BPRO215
BARG301
BARG304

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGKGGFGVVFrAhhrtwnhd..........VAVK
ChainResidueDetails
AVAL28-LYS51

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LlHrDLKpsNILL
ChainResidueDetails
ALEU139-LEU151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU198

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING:
ChainResidueDetails
BLYS219

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by RIPK3 => ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729
ChainResidueDetails
BSER345
BSER347

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by RIPK3 => ECO:0000269|PubMed:24012422, ECO:0000269|PubMed:24095729
ChainResidueDetails
BTHR349
ASER165
ASER304

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by RIPK3 => ECO:0000269|PubMed:24095729
ChainResidueDetails
BSER352

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q9Y572
ChainResidueDetails
ASER204

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:23612963, ECO:0000269|PubMed:27819682
ChainResidueDetails
ATPO231

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:23612963, ECO:0000269|PubMed:27819682
ChainResidueDetails
ASEP232

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:23612963
ChainResidueDetails
ATHR257

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PDB entries from 2024-07-24

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