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3FL3

X-ray structure of the ligand free non covalent swapped form of the A19P/Q28L/K31C/S32C mutant of bovine pancreatic ribonuclease

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 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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS12
BHIS12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS119
BHIS119

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ALYS7
BARG85
AARG10
ALYS41
ALYS66
AARG85
BLYS7
BARG10
BLYS41
BLYS66

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: N-linked (Glc) (glycation) lysine; in vitro => ECO:0000269|PubMed:4030761
ChainResidueDetails
ALYS1
ALYS7
ALYS37
ALYS41
BLYS1
BLYS7
BLYS37
BLYS41

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:19358553
ChainResidueDetails
AASN34
BASN34

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 2025-06-25

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