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4BSZ

Crystal Structure of the Yeast Ribosomal Protein Rps3 in Complex with its Chaperone Yar1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000054biological_processribosomal subunit export from nucleus
A0000056biological_processribosomal small subunit export from nucleus
A0002181biological_processcytoplasmic translation
A0003723molecular_functionRNA binding
A0003735molecular_functionstructural constituent of ribosome
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005840cellular_componentribosome
A0006412biological_processtranslation
A0015935cellular_componentsmall ribosomal subunit
A0022626cellular_componentcytosolic ribosome
A0022627cellular_componentcytosolic small ribosomal subunit
A0030686cellular_component90S preribosome
A0030688cellular_componentpreribosome, small subunit precursor
A0070651biological_processnonfunctional rRNA decay
A1990145biological_processmaintenance of translational fidelity
A1990904cellular_componentribonucleoprotein complex
B0000056biological_processribosomal small subunit export from nucleus
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006970biological_processresponse to osmotic stress
B0030907cellular_componentMBF transcription complex
B0032880biological_processregulation of protein localization
B0033309cellular_componentSBF transcription complex
B0034599biological_processcellular response to oxidative stress
B0042274biological_processribosomal small subunit biogenesis
B0051082molecular_functionunfolded protein binding
Functional Information from PROSITE/UniProt
site_idPS00548
Number of Residues37
DetailsRIBOSOMAL_S3 Ribosomal protein S3 signature. AKamkfadGfLihSgqpVndfIDtatrhvlMrqGvlG
ChainResidueDetails
AALA147-GLY183

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950
ChainResidueDetails
BSER78

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17287358
ChainResidueDetails
ATHR70

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER97

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
ASER129

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine; by SFM1 => ECO:0000269|PubMed:22650761
ChainResidueDetails
AARG146

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER221

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR231

site_idSWS_FT_FI8
Number of Residues5
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS106
ALYS132
ALYS141
ALYS151
ALYS200

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:28757607, ECO:0000269|PubMed:30718516, ECO:0000269|PubMed:30893611, ECO:0000269|PubMed:31819057, ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS212

225946

PDB entries from 2024-10-09

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