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2HKY

NMR solution structure of human RNase 7

Functional Information from GO Data
ChainGOidnamespacecontents
A0001530molecular_functionlipopolysaccharide binding
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004540molecular_functionRNA nuclease activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0019731biological_processantibacterial humoral response
A0042742biological_processdefense response to bacterium
A0042834molecular_functionpeptidoglycan binding
A0045087biological_processinnate immune response
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0050832biological_processdefense response to fungus
A0051715biological_processcytolysis in another organism
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKdlNTF
ChainResidueDetails
ACYS37-PHE43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsRegion: {"description":"Important for antibacterial activity","evidences":[{"source":"PubMed","id":"17150966","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17150966","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"17150966","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P15468","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Critical for catalytic activity","evidences":[{"source":"PubMed","id":"17150966","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4y
ChainResidueDetails
ALYS38
AHIS15
AHIS123

246704

PDB entries from 2025-12-24

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