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6QMN

Crystal structure of a Ribonuclease A-Onconase chimera

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004522molecular_functionribonuclease A activity
A0004540molecular_functionRNA nuclease activity
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
B0005576cellular_componentextracellular region
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0050830biological_processdefense response to Gram-positive bacterium
C0003676molecular_functionnucleic acid binding
C0004518molecular_functionnuclease activity
C0004519molecular_functionendonuclease activity
C0004522molecular_functionribonuclease A activity
C0004540molecular_functionRNA nuclease activity
C0005576cellular_componentextracellular region
C0016787molecular_functionhydrolase activity
C0016829molecular_functionlyase activity
C0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue PO4 A 500
ChainResidue
AGLN11
AHIS12
ALYS41
AHIS117
APHE118
AHOH625
AHOH638

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 B 500
ChainResidue
BLYS41
BHIS117
BPHE118
BHOH623
BGLN11
BHIS12

site_idAC3
Number of Residues6
Detailsbinding site for residue PO4 C 500
ChainResidue
CGLN11
CHIS12
CLYS41
CHIS117
CPHE118
CHOH617

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 Residues63
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues24
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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