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4WW5

Crystal structure of binary complex Bud32-Cgi121 in complex with AMPP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000282biological_processcellular bud site selection
A0000408cellular_componentEKC/KEOPS complex
A0000722biological_processtelomere maintenance via recombination
A0000723biological_processtelomere maintenance
A0000781cellular_componentchromosome, telomeric region
A0002949biological_processtRNA threonylcarbamoyladenosine modification
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006468biological_processprotein phosphorylation
A0008033biological_processtRNA processing
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0070525biological_processtRNA threonylcarbamoyladenosine metabolic process
A0106310molecular_functionprotein serine kinase activity
A1990145biological_processmaintenance of translational fidelity
B0000049molecular_functiontRNA binding
B0000408cellular_componentEKC/KEOPS complex
B0000722biological_processtelomere maintenance via recombination
B0000723biological_processtelomere maintenance
B0000781cellular_componentchromosome, telomeric region
B0002949biological_processtRNA threonylcarbamoyladenosine modification
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0006310biological_processDNA recombination
B0008033biological_processtRNA processing
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B1990145biological_processmaintenance of translational fidelity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ANP A 301
ChainResidue
AILE50
AGLY184
AHOH470
AHOH479
ALYS52
AARG72
AGLU107
APHE108
ALEU109
APHE119
AASP182
APHE183

site_idAC2
Number of Residues4
Detailsbinding site for residue ACT A 302
ChainResidue
ALEU199
AGLU203
AASN218
AILE221

site_idAC3
Number of Residues3
Detailsbinding site for residue ACT A 303
ChainResidue
AGLU203
ALEU207
AARG251

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 304
ChainResidue
ASER135
AASP136
AARG253
AARG257
AHOH405

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 305
ChainResidue
AARG143
ALYS216
ATRP220
AGLU223

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 306
ChainResidue
ACYS90
AVAL91
AGLU107
AHIS179
AHOH480
BARG170

site_idAC7
Number of Residues4
Detailsbinding site for residue ACT B 201
ChainResidue
BTYR145
BGLU147
BGLN163
BASP164

site_idAC8
Number of Residues8
Detailsbinding site for residue SO4 B 204
ChainResidue
ATYR100
BGLU63
BASN67
BARG70
BARG143
BHOH304
BHOH305
BHOH306

site_idAC9
Number of Residues6
Detailsbinding site for residues SO4 B 202 and SO4 B 203
ChainResidue
BLYS68
BILE134
BGLU135
BASN140
BHOH307
BHOH357

Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YCHgDLTSSNIVL
ChainResidueDetails
ATYR157-LEU169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"12023889","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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