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3FL0

X-ray structure of the non covalent swapped form of the Q28L/K31C/S32C mutant of bovine pancreatic ribonuclease in complex with 2'-DEOXYCYTIDINE-2'-DEOXYGUANOSINE-3',5'-MONOPHOSPHATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004522molecular_functionribonuclease A activity
A0004540molecular_functionRNA nuclease activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0050830biological_processdefense response to Gram-positive bacterium
B0003676molecular_functionnucleic acid binding
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004522molecular_functionribonuclease A activity
B0004540molecular_functionRNA nuclease activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CGP A 900
ChainResidue
ALYS41
BHOH903
AVAL43
AASN44
ATHR45
AHIS119
APHE120
AHOH659
BGLN11
BHIS12

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF
ChainResidueDetails
ACYS40-PHE46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"4030761","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","featureId":"CAR_000006","evidences":[{"source":"PubMed","id":"19358553","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
APHE120
AHIS119
AHIS12
ALYS41

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
BPHE120
BHIS119
BHIS12
BLYS41

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
AHIS119
AHIS12
ALYS41

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
BHIS119
BHIS12
BLYS41

site_idMCSA1
Number of Residues2
DetailsM-CSA 164
ChainResidueDetails
AHIS12hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU49electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 164
ChainResidueDetails
BHIS12hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLU49electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-10-22

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