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1Q8Z

The apoenzyme structure of the yeast SR protein kinase, Sky1p

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 Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
AHOH101
APRO152
ATYR153
ALYS154
AASP155
APHE232
AASN233
AHIS234
ALYS235

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 802
ChainResidue
BPRO152
BLYS154
BASP155
BASN233
BHIS234
BLYS235

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1000
ChainResidue
AALA198
AASP201
AGLY552
AALA554
ATYR561
AMOH2390

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 1003
ChainResidue
AHOH34
BALA198
BASP201
BGLY552
BALA554
BTYR561
BMOH2389

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MOH B 2389
ChainResidue
AGLU197
AMOH2390
BEDO1003

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MOH A 2390
ChainResidue
AEDO1000
BMOH2389

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGWGHFSTVWlAkdmvnnth..........VAMK
ChainResidueDetails
ALEU164-LYS187

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHtDIKpeNVLM
ChainResidueDetails
AILE290-MET302

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP294
BASP294

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU164
ALYS187
BLEU164
BLYS187

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
AASP615
BASP615

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
AHIS618
BHIS618

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
AALA620
ATHR642
ATRP659
BALA620
BTHR642
BTRP659

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ALEU625
AASP681
APRO685
BLEU625
BASP681
BPRO685

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
AVAL664
ALYS677
BVAL664
BLYS677

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AGLU298
AASP294

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BGLU298
BASP294

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP294
ALYS296

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP294
BLYS296

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR567
AASP294
ALYS296

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR567
BASP294
BLYS296

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP294
ALYS296
AASN299

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP294
BLYS296
BASN299

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PDB entries from 2024-10-30

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