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5D9H

Crystal structure of SPAK (STK39) dimer in the basal activity state

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 Residues16
Detailsbinding site for residue ATP A 501
ChainResidue
AILE81
AASP204
ALYS206
AGLY208
AASN209
ALEU211
AASP222
AMG502
AVAL89
AALA102
ALYS104
AMET150
ALYS151
ALEU153
ASER157
AASP160

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 502
ChainResidue
ALYS104
AASN209
AASP222
AATP501

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 503
ChainResidue
AGLY319
ALYS320
ASER321
ALYS351

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 504
ChainResidue
AASN354
AARG355

site_idAC5
Number of Residues16
Detailsbinding site for residue ATP B 501
ChainResidue
BILE81
BGLY82
BALA102
BLYS104
BLYS151
BLEU153
BSER157
BLEU159
BASP160
BASP204
BLYS206
BGLY208
BASN209
BLEU211
BASP222
BMG502

site_idAC6
Number of Residues3
Detailsbinding site for residue MG B 502
ChainResidue
BASN209
BASP222
BATP501

site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 B 503
ChainResidue
BGLY319
BLYS320
BSER321

site_idAC8
Number of Residues2
Detailsbinding site for residue SO4 B 504
ChainResidue
BASN354
BARG355

site_idAC9
Number of Residues1
Detailsbinding site for residue SO4 B 505
ChainResidue
BLYS186

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGATAVVQaAlckprqer..........VAIK
ChainResidueDetails
AILE81-LYS104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"16382158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKC/PRKCQ","evidences":[{"source":"UniProtKB","id":"Q9UEW8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9UEW8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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