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4M5D

Crystal structure of the Utp22 and Rrp7 complex from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000028biological_processribosomal small subunit assembly
A0003674molecular_functionmolecular_function
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0006364biological_processrRNA processing
A0006409biological_processtRNA export from nucleus
A0030490biological_processmaturation of SSU-rRNA
A0030686cellular_component90S preribosome
A0032040cellular_componentsmall-subunit processome
A0032545cellular_componentCURI complex
A0034456cellular_componentUTP-C complex
A0042254biological_processribosome biogenesis
A0042790biological_processnucleolar large rRNA transcription by RNA polymerase I
A0060962biological_processregulation of ribosomal protein gene transcription by RNA polymerase II
A1990904cellular_componentribonucleoprotein complex
B0000028biological_processribosomal small subunit assembly
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0006364biological_processrRNA processing
B0019843molecular_functionrRNA binding
B0030490biological_processmaturation of SSU-rRNA
B0032040cellular_componentsmall-subunit processome
B0032545cellular_componentCURI complex
B0034456cellular_componentUTP-C complex
B0042254biological_processribosome biogenesis
B0042790biological_processnucleolar large rRNA transcription by RNA polymerase I
B0060962biological_processregulation of ribosomal protein gene transcription by RNA polymerase II
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1301
ChainResidue
ALYS192
ATYR350
ALYS353
ALYS354
AHOH1763

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1302
ChainResidue
AHOH1493
AHOH1930
ASER376
ASER377
AGLY389
ATHR390

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1303
ChainResidue
ASER384
ALEU385
AHOH1424
AHOH1890

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1304
ChainResidue
ALEU574
AGLY575
AASP576
AARG577
ALYS626
ATHR629
ALYS630
AHOH1411

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1305
ChainResidue
ALYS166
AARG597
ATYR600

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1306
ChainResidue
AARG656
APHE658
ALYS659

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1307
ChainResidue
AHIS923
AARG1063
ALEU1067
APRO1091
AGLY1092
ALEU1093
AHOH1658

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1308
ChainResidue
AHIS1194
ALYS1195
AARG1197

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1309
ChainResidue
AARG822
AHOH1556

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1310
ChainResidue
ALYS410
AHIS414
AILE861
AARG865
AHOH1440
AHOH1968

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1311
ChainResidue
AARG92
AGLU96
ALYS423
ALYS427
AASN500

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 1312
ChainResidue
ATRP968
AASN969
ALYS971
ATHR1065
ALYS1069

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGE A 1313
ChainResidue
ALYS115
ALYS117
AGLN118
ALYS119
ALYS119

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PGE B 301
ChainResidue
ATYR1152
BPHE93
BPHE171

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER10

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER58
ASER64

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR60

222036

PDB entries from 2024-07-03

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