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1B2M

THREE-DIMENSIONAL STRUCTURE OF RIBONULCEASE T1 COMPLEXED WITH AN ISOSTERIC PHOSPHONATE ANALOGUE OF GPU: ALTERNATE SUBSTRATE BINDING MODES AND CATALYSIS.

Functional Information from GO Data
ChainGOidnamespacecontents
A0001411cellular_componenthyphal tip
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0004540molecular_functionRNA nuclease activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0030428cellular_componentcell septum
A0046589molecular_functionribonuclease T1 activity
B0001411cellular_componenthyphal tip
B0003723molecular_functionRNA binding
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004521molecular_functionRNA endonuclease activity
B0004540molecular_functionRNA nuclease activity
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0030428cellular_componentcell septum
B0046589molecular_functionribonuclease T1 activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"2844811","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"2844811","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues6
Detailsa catalytic site defined by CSA, PubMed 10029539, 20088566, 11048955
ChainResidueDetails
ATYR38
AHIS40
AGLU58
AARG77
AHIS92
APHE100

site_idMCSA1
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails

site_idMCSA2
Number of Residues6
DetailsM-CSA 414
ChainResidueDetails

238895

PDB entries from 2025-07-16

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