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1BOL

THE CRYSTAL STRUCTURE OF RIBONUCLEASE RH FROM RHIZOPUS NIVEUS AT 2.0 A RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0005576cellular_componentextracellular region
A0006401biological_processRNA catabolic process
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0033897molecular_functionribonuclease T2 activity
Functional Information from PDB Data
site_idACT
Number of Residues3
DetailsACTIVE SITE
ChainResidue
AHIS46
AHIS109
AGLU105

Functional Information from PROSITE/UniProt
site_idPS00530
Number of Residues8
DetailsRNASE_T2_1 Ribonuclease T2 family histidine active site 1. FtLHGLWP
ChainResidueDetails
APHE43-PRO50

site_idPS00531
Number of Residues12
DetailsRNASE_T2_2 Ribonuclease T2 family histidine active site 2. FwsHEWsKHGtC
ChainResidueDetails
APHE101-CYS112

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"evidences":[{"source":"PubMed","id":"8551522","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 8551522
ChainResidueDetails
AHIS109
AHIS46
AGLU105

site_idMCSA1
Number of Residues6
DetailsM-CSA 426
ChainResidueDetails
AHIS46proton shuttle (general acid/base)
ATRP49electrostatic stabiliser, modifies pKa, steric role
ATYR57electrostatic stabiliser
AGLU105modifies pKa
ALYS108electrostatic stabiliser
AHIS109proton shuttle (general acid/base)

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PDB entries from 2026-02-25

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