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1O0N

Ribonuclease A in complex with uridine-3'-phosphate

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 Residues15
DetailsBINDING SITE FOR RESIDUE U3P A 1101
ChainResidue
AGLN11
AHOH1118
AHOH1190
AHOH1191
AHOH1212
AHOH1213
AHOH1274
AHIS12
ALYS41
AVAL43
AASN44
ATHR45
AHIS119
APHE120
AHOH1117

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE U3P B 1201
ChainResidue
BGLN11
BHIS12
BLYS41
BVAL43
BASN44
BTHR45
BHIS119
BPHE120
BHOH1213
BHOH1214
BHOH1224
BHOH1227
BHOH1228
BHOH1229
BHOH1387

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 Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"4030761","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
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 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

238895

PDB entries from 2025-07-16

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