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5J0A

Crystal structure of PDZ-binding kinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000278biological_processmitotic cell cycle
A0001933biological_processnegative regulation of protein phosphorylation
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004708molecular_functionMAP kinase kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0006468biological_processprotein phosphorylation
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032873biological_processnegative regulation of stress-activated MAPK cascade
A0034644biological_processcellular response to UV
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0050728biological_processnegative regulation of inflammatory response
A0051403biological_processstress-activated MAPK cascade
A0106310molecular_functionprotein serine kinase activity
B0000278biological_processmitotic cell cycle
B0001933biological_processnegative regulation of protein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004708molecular_functionMAP kinase kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0006468biological_processprotein phosphorylation
B0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
B0032873biological_processnegative regulation of stress-activated MAPK cascade
B0034644biological_processcellular response to UV
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0050728biological_processnegative regulation of inflammatory response
B0051403biological_processstress-activated MAPK cascade
B0106310molecular_functionprotein serine kinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue SO4 A 401
ChainResidue
ASER76

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 402
ChainResidue
AARG81
AGLY188
AVAL189
ASER190

site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 403
ChainResidue
ALYS176
AGLY177
ATYR117
AGLY119
AGLU120
AILE175

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 404
ChainResidue
AARG130
APRO139

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 405
ChainResidue
AHIS94
AARG152
AVAL315

site_idAC6
Number of Residues8
Detailsbinding site for residue HC4 A 406
ChainResidue
ALYS65
AILE66
AASN67
APRO68
AHOH521
BTHR209
BGLU210
BTYR272

site_idAC7
Number of Residues8
Detailsbinding site for residue HC4 A 407
ChainResidue
ATYR78
AARG101
AGLU116
ATYR117
BTYR78
BARG101
BPHE103
BLYS306

site_idAC8
Number of Residues8
Detailsbinding site for residue HC4 A 408
ChainResidue
ATHR209
AGLU210
ATYR272
AHOH505
BLYS65
BILE66
BASN67
BPRO68

site_idAC9
Number of Residues4
Detailsbinding site for residue SO4 B 401
ChainResidue
BARG81
BGLY188
BVAL189
BSER190

site_idAD1
Number of Residues4
Detailsbinding site for residue SO4 B 402
ChainResidue
ASER76
AGLN79
BHIS73
BSER76

site_idAD2
Number of Residues5
Detailsbinding site for residue SO4 B 403
ChainResidue
BILE69
BARG75
BGLN79
BLYS80
BHOH530

site_idAD3
Number of Residues3
Detailsbinding site for residue SO4 B 404
ChainResidue
BHIS93
BHIS94
BPRO95

site_idAD4
Number of Residues3
Detailsbinding site for residue SO4 B 405
ChainResidue
BARG278
BASN302
BGLU303

site_idAD5
Number of Residues7
Detailsbinding site for residue HC4 B 406
ChainResidue
BLYS90
BARG101
BALA102
BTHR104
BGLU105
BGLU219
BASP304

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LlHgDIKssNVVI
ChainResidueDetails
ALEU163-ILE175
BLEU163-ILE175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
BASP167

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
BLEU38
BLYS64

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BTHR24

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER32

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER59

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS169

223532

PDB entries from 2024-08-07

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