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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
A0004519molecular_functionendonuclease activity
A0004540molecular_functionRNA nuclease activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17150966
ChainResidueDetails
AHIS15

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:17150966
ChainResidueDetails
AHIS123

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P15468
ChainResidueDetails
AASN41
ATHR42
AHIS123
AARG126
AHIS15
ALYS38

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Critical for catalytic activity => ECO:0000269|PubMed:17150966
ChainResidueDetails
ALYS38

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN99

219869

PDB entries from 2024-05-15

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