Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4KRC

Crystal Structure of Pho85-Pcl10-ATP-gamma-S Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0001676biological_processlong-chain fatty acid metabolic process
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005935cellular_componentcellular bud neck
A0005979biological_processregulation of glycogen biosynthetic process
A0006355biological_processregulation of DNA-templated transcription
A0006357biological_processregulation of transcription by RNA polymerase II
A0006468biological_processprotein phosphorylation
A0006974biological_processDNA damage response
A0009891biological_processpositive regulation of biosynthetic process
A0016239biological_processpositive regulation of macroautophagy
A0016242biological_processnegative regulation of macroautophagy
A0019216biological_processregulation of lipid metabolic process
A0030952biological_processestablishment or maintenance of cytoskeleton polarity
A0031505biological_processfungal-type cell wall organization
A0031647biological_processregulation of protein stability
A0032878biological_processregulation of establishment or maintenance of cell polarity
A0032880biological_processregulation of protein localization
A0044843biological_processcell cycle G1/S phase transition
A0045719biological_processnegative regulation of glycogen biosynthetic process
A0045936biological_processnegative regulation of phosphate metabolic process
A0046822biological_processregulation of nucleocytoplasmic transport
A0050849biological_processnegative regulation of calcium-mediated signaling
A0051302biological_processregulation of cell division
A0051726biological_processregulation of cell cycle
A0055088biological_processlipid homeostasis
A0071073biological_processpositive regulation of phospholipid biosynthetic process
A0106310molecular_functionprotein serine kinase activity
A1901987biological_processregulation of cell cycle phase transition
A1902554cellular_componentserine/threonine protein kinase complex
A1990860cellular_componentPho85-Pho80 CDK-cyclin complex
B0000079biological_processregulation of cyclin-dependent protein serine/threonine kinase activity
B0019901molecular_functionprotein kinase binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASN138
AASP151
AAGS402

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AGS A 402
ChainResidue
AGLU83
AMET85
AASP88
AASP133
ALYS135
AGLN137
AASN138
ALEU140
AASP151
AMG401
AHOH504
AGLY16
ATHR17
ATYR18
AVAL21
AALA34
ALYS36

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGNGTYATVYkGlnkttgvy..........VALK
ChainResidueDetails
ALEU13-LYS36

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDLKpqNLLI
ChainResidueDetails
AILE129-ILE141

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
AASP133

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALYS36
ALEU13

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Not phosphorylated => ECO:0000269|PubMed:10490639
ChainResidueDetails
ASER167
ASER166

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:10620010
ChainResidueDetails
ATYR18

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS289

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon