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5ULJ

Crystal structure of Scheffersomyces stipitis Rai1 in complex with (3'-NADP)+ and calcium ion

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000956biological_processnuclear-transcribed mRNA catabolic process
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0005634cellular_componentnucleus
A0005829cellular_componentcytosol
A0006397biological_processmRNA processing
A0034353molecular_functionmRNA 5'-diphosphatase activity
A0046872molecular_functionmetal ion binding
A0110155biological_processNAD-cap decapping
B0000166molecular_functionnucleotide binding
B0000956biological_processnuclear-transcribed mRNA catabolic process
B0003723molecular_functionRNA binding
B0004518molecular_functionnuclease activity
B0005634cellular_componentnucleus
B0005829cellular_componentcytosol
B0006397biological_processmRNA processing
B0034353molecular_functionmRNA 5'-diphosphatase activity
B0046872molecular_functionmetal ion binding
B0110155biological_processNAD-cap decapping
C0000166molecular_functionnucleotide binding
C0000956biological_processnuclear-transcribed mRNA catabolic process
C0003723molecular_functionRNA binding
C0004518molecular_functionnuclease activity
C0005634cellular_componentnucleus
C0005829cellular_componentcytosol
C0006397biological_processmRNA processing
C0034353molecular_functionmRNA 5'-diphosphatase activity
C0046872molecular_functionmetal ion binding
C0110155biological_processNAD-cap decapping
D0000166molecular_functionnucleotide binding
D0000956biological_processnuclear-transcribed mRNA catabolic process
D0003723molecular_functionRNA binding
D0004518molecular_functionnuclease activity
D0005634cellular_componentnucleus
D0005829cellular_componentcytosol
D0006397biological_processmRNA processing
D0034353molecular_functionmRNA 5'-diphosphatase activity
D0046872molecular_functionmetal ion binding
D0110155biological_processNAD-cap decapping
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue CA A 401
ChainResidue
AGLU179
AASP230
AGLU249
ALEU250
A0WD402
AHOH504
AHOH505
AHOH512

site_idAC2
Number of Residues16
Detailsbinding site for residue 0WD A 402
ChainResidue
AMET77
ATYR107
AARG108
AGLY109
ATYR176
AGLN209
AALA226
AGLY227
AGLU228
ALYS251
AGLN275
ACA401
AHOH522
AHOH543
AHOH669
AASN76

site_idAC3
Number of Residues7
Detailsbinding site for residue CA B 401
ChainResidue
BASP230
BGLU249
BLEU250
B0WD402
BHOH521
BHOH540
BHOH604

site_idAC4
Number of Residues29
Detailsbinding site for residue 0WD B 402
ChainResidue
BGLU73
BASN76
BMET77
BTYR107
BARG108
BGLY109
BSER140
BGLU145
BTYR176
BASN206
BGLN209
BGLY227
BGLU228
BGLU249
BLYS251
BCA401
BHOH503
BHOH506
BHOH520
BHOH521
BHOH525
BHOH551
BHOH560
BHOH601
BHOH604
BHOH617
BHOH658
BHOH689
BHOH691

site_idAC5
Number of Residues5
Detailsbinding site for residue PPV C 401
ChainResidue
CARG108
CGLY109
CGLY227
CGLU228
CHOH513

site_idAC6
Number of Residues8
Detailsbinding site for residue PPV D 401
ChainResidue
DTYR107
DARG108
DGLY109
DALA226
DGLY227
DGLU228
DGLN275
DHOH517

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:28283058, ECO:0007744|PDB:5ULJ
ChainResidueDetails
ATYR107
BGLU179
BGLU228
BASP230
BGLU249
BLEU250
BLYS251
BGLN275
CTYR107
CGLU179
CGLU228
AGLU179
CASP230
CGLU249
CLEU250
CLYS251
CGLN275
DTYR107
DGLU179
DGLU228
DASP230
DGLU249
AGLU228
DLEU250
DLYS251
DGLN275
AASP230
AGLU249
ALEU250
ALYS251
AGLN275
BTYR107

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PDB entries from 2024-06-05

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