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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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP204
BASP204

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE81
ALYS104
BILE81
BLYS104

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by WNK4 => ECO:0000269|PubMed:16382158, ECO:0000269|PubMed:16530727, ECO:0000269|PubMed:21486947
ChainResidueDetails
ATHR243
BTHR243

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:16382158
ChainResidueDetails
ATHR247
BTHR247

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKC/PRKCQ => ECO:0000250|UniProtKB:Q9UEW8
ChainResidueDetails
ASER321
BSER321

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9UEW8
ChainResidueDetails
ALYS361
BLYS361

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:21733846
ChainResidueDetails
ATHR366
BTHR366

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9UEW8
ChainResidueDetails
ASER382
BSER382

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21733846
ChainResidueDetails
ASER383
BSER383

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER397
BSER397

227344

PDB entries from 2024-11-13

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