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5NJ7

The X-ray structure of the adduct formed in the reaction between bovine pancreatic ribonuclease and arsenoplatin-1

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 Residues5
Detailsbinding site for residue A6R A 201
ChainResidue
ATHR78
AHIS105
AASN113
APRO114
AHOH357

site_idAC2
Number of Residues6
Detailsbinding site for residue A6R A 202
ChainResidue
AHOH313
AHOH322
ALYS7
AGLN11
ALYS41
AHIS119

site_idAC3
Number of Residues9
Detailsbinding site for residue A6R B 201
ChainResidue
BLYS7
BGLN11
BLYS41
BVAL118
BHIS119
BHOH326
BHOH330
BHOH338
BHOH351

site_idAC4
Number of Residues3
Detailsbinding site for residue A6R B 202
ChainResidue
BTHR78
BHIS105
BHOH323

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_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 2025-07-30

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