Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5BUD

Crystal structure of Candida albicans Rai1 in complex with pU5-Mn2+

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000448biological_processcleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0000463biological_processmaturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0000466biological_processmaturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
A0000956biological_processnuclear-transcribed mRNA catabolic process
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006397biological_processmRNA processing
A0016787molecular_functionhydrolase activity
A0030234molecular_functionenzyme regulator activity
A0030846biological_processtermination of RNA polymerase II transcription, poly(A)-coupled
A0031087biological_processdeadenylation-independent decapping of nuclear-transcribed mRNA
A0034353molecular_functionmRNA 5'-diphosphatase activity
A0046872molecular_functionmetal ion binding
A0071035biological_processnuclear polyadenylation-dependent rRNA catabolic process
A0090730cellular_componentLas1 complex
A0110103cellular_componentRNA polymerase II termination complex
A0110152molecular_functionRNA NAD+-cap (NAD+-forming) hydrolase activity
A0110155biological_processNAD-cap decapping
A1904595biological_processpositive regulation of termination of RNA polymerase II transcription
A1990174molecular_functionphosphodiesterase decapping endonuclease activity
B0000166molecular_functionnucleotide binding
B0000448biological_processcleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0000463biological_processmaturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0000466biological_processmaturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
B0000956biological_processnuclear-transcribed mRNA catabolic process
B0003723molecular_functionRNA binding
B0004518molecular_functionnuclease activity
B0005634cellular_componentnucleus
B0005829cellular_componentcytosol
B0006397biological_processmRNA processing
B0016787molecular_functionhydrolase activity
B0030234molecular_functionenzyme regulator activity
B0030846biological_processtermination of RNA polymerase II transcription, poly(A)-coupled
B0031087biological_processdeadenylation-independent decapping of nuclear-transcribed mRNA
B0034353molecular_functionmRNA 5'-diphosphatase activity
B0046872molecular_functionmetal ion binding
B0071035biological_processnuclear polyadenylation-dependent rRNA catabolic process
B0090730cellular_componentLas1 complex
B0110103cellular_componentRNA polymerase II termination complex
B0110152molecular_functionRNA NAD+-cap (NAD+-forming) hydrolase activity
B0110155biological_processNAD-cap decapping
B1904595biological_processpositive regulation of termination of RNA polymerase II transcription
B1990174molecular_functionphosphodiesterase decapping endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 401
ChainResidue
AASP225
AGLU244
ALEU245
AMN402
AHOH581
DU2

site_idAC2
Number of Residues6
Detailsbinding site for residue MN A 402
ChainResidue
AHOH599
AHOH628
DU2
AGLU223
AASP225
AMN401

site_idAC3
Number of Residues7
Detailsbinding site for residue MN A 403
ChainResidue
AGLU174
AGLU223
AHOH524
AHOH563
AHOH628
AHOH737
AHOH898

site_idAC4
Number of Residues6
Detailsbinding site for residue MN B 401
ChainResidue
BASP225
BGLU244
BLEU245
BMN402
BHOH582
EU2

site_idAC5
Number of Residues7
Detailsbinding site for residue MN B 402
ChainResidue
BGLU223
BASP225
BMN401
BHOH556
BHOH610
BHOH860
EU2

site_idAC6
Number of Residues7
Detailsbinding site for residue MN B 403
ChainResidue
BGLU174
BGLU223
BHOH546
BHOH610
BHOH625
BHOH863
BHOH946

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26101253","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BTH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5BUD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O70348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon