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3AHS

Crystal Structure of Ustilago sphaerogena Ribonuclease U2B

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0004540molecular_functionRNA nuclease activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0033899molecular_functionribonuclease U2 activity
A0046872molecular_functionmetal ion binding
B0003723molecular_functionRNA binding
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004521molecular_functionRNA endonuclease activity
B0004540molecular_functionRNA nuclease activity
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0033899molecular_functionribonuclease U2 activity
B0046872molecular_functionmetal ion binding
C0003723molecular_functionRNA binding
C0004518molecular_functionnuclease activity
C0004519molecular_functionendonuclease activity
C0004521molecular_functionRNA endonuclease activity
C0004540molecular_functionRNA nuclease activity
C0016787molecular_functionhydrolase activity
C0016829molecular_functionlyase activity
C0033899molecular_functionribonuclease U2 activity
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 115
ChainResidue
ATYR39
CTYR78
AHIS41
AGLU62
AARG85
AHIS101
APHE110
AHOH247
AHOH382
AHOH488

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 116
ChainResidue
AASP28
AVAL30
AGLY33
AHOH505

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 B 115
ChainResidue
BTYR39
BHIS41
BGLU62
BTYR78
BARG85
BHIS101
BPHE110
BHOH258
BHOH282
BHOH390

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 116
ChainResidue
BASP28
BVAL30
BGLY33
BHOH427

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 C 115
ChainResidue
ATYR78
CTYR39
CHIS41
CGLU62
CARG85
CHIS101
CPHE110
CHOH305
CHOH320
CHOH438

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GOL C 201
ChainResidue
BGLY10
BTHR102
BGLY103
BTHR111
CGLY10
CGLY11
CASN12
CTHR102
CHOH294
CHOH329
CHOH367
CHOH481

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 202
ChainResidue
ATYR44
AGLU46
AHOH437

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1973","firstPage":"453","lastPage":"472","publisher":"Publ. House Slovak Acad. Sci.","address":"Bratislava","bookName":"Ribosomes and RNA metabolism","editors":["Zelinka J.","Balan J."],"authors":["Uchida T.","Sato S."]}}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1973","firstPage":"453","lastPage":"472","publisher":"Publ. House Slovak Acad. Sci.","address":"Bratislava","bookName":"Ribosomes and RNA metabolism","editors":["Zelinka J.","Balan J."],"authors":["Uchida T.","Sato S."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1973","firstPage":"453","lastPage":"472","publisher":"Publ. House Slovak Acad. Sci.","address":"Bratislava","bookName":"Ribosomes and RNA metabolism","editors":["Zelinka J.","Balan J."],"authors":["Uchida T.","Sato S."]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20858208","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues39
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsSite: {"description":"Methylation inactivates enzyme","evidences":[{"source":"PubMed","id":"7492561","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 908
ChainResidueDetails
AASP45proton shuttle (general acid/base)
AVAL66proton shuttle (general acid/base)
AGLN89electrostatic stabiliser
AALA105proton shuttle (general acid/base)

site_idMCSA2
Number of Residues4
DetailsM-CSA 908
ChainResidueDetails
BASP45proton shuttle (general acid/base)
BVAL66proton shuttle (general acid/base)
BGLN89electrostatic stabiliser
BALA105proton shuttle (general acid/base)

site_idMCSA3
Number of Residues4
DetailsM-CSA 908
ChainResidueDetails
CASP45proton shuttle (general acid/base)
CVAL66proton shuttle (general acid/base)
CGLN89electrostatic stabiliser
CALA105proton shuttle (general acid/base)

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PDB entries from 2025-07-23

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