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1B6V

CRYSTAL STRUCTURE OF A HYBRID BETWEEN RIBONUCLEASE A AND BOVINE SEMINAL RIBONUCLEASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004519molecular_functionendonuclease activity
A0004522molecular_functionribonuclease A activity
A0004540molecular_functionRNA nuclease activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0016829molecular_functionlyase activity
A0050830biological_processdefense response to Gram-positive bacterium
B0003676molecular_functionnucleic acid binding
B0004519molecular_functionendonuclease activity
B0004522molecular_functionribonuclease A activity
B0004540molecular_functionRNA nuclease activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
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 Residues5
DetailsM-CSA 164
ChainResidueDetails
AHIS12hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS41electrostatic stabiliser, hydrogen bond donor
AHIS119hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
APHE120electrostatic stabiliser, hydrogen bond donor
AASP121electrostatic stabiliser, hydrogen bond acceptor

site_idMCSA2
Number of Residues5
DetailsM-CSA 164
ChainResidueDetails
BHIS12hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BLYS41electrostatic stabiliser, hydrogen bond donor
BHIS119hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BPHE120electrostatic stabiliser, hydrogen bond donor
BASP121electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2024-10-30

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