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4RSD

STRUCTURE OF THE D121A VARIANT OF RIBONUCLEASE A

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 125
ChainResidue
AGLN11
AHIS12
AVAL118
AHIS119
APHE120
AHOH166

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 126
ChainResidue
AARG10
AASN34
ATHR78

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 127
ChainResidue
AHIS12
AASN44
ATHR45

site_idB1
Number of Residues2
DetailsPYRIMIDINE BINDING SITE ON 5' SIDE OF SCISSILE PHOSPHATE.
ChainResidue
ATHR45
AASP83

site_idB2
Number of Residues2
DetailsPURINE BINDING SITE ON 3' SIDE OF SCISSILE PHOSPHATE.
ChainResidue
AASN71
AGLU111

site_idP1
Number of Residues3
DetailsCATALYZES CLEAVAGE OF THE P-O5' BOND OF A PHOSPHORYL GROUP IN THIS SUBSITE.
ChainResidue
AHIS12
AHIS119
ALYS41

site_idP2
Number of Residues2
DetailsPHOSPHATE BINDING SITE.
ChainResidue
ALYS7
AARG10

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 Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"4030761","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
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 Residues3
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
AHIS119
AHIS12
ALYS41

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
AALA121electrostatic stabiliser, hydrogen bond acceptor

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PDB entries from 2025-07-16

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