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1RNF

X-RAY CRYSTAL STRUCTURE OF UNLIGANDED HUMAN RIBONUCLEASE 4

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
A0005615cellular_componentextracellular space
A0016787molecular_functionhydrolase activity
A0019731biological_processantibacterial humoral response
A0042742biological_processdefense response to bacterium
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
B0005615cellular_componentextracellular space
B0016787molecular_functionhydrolase activity
B0019731biological_processantibacterial humoral response
B0042742biological_processdefense response to bacterium
B0050830biological_processdefense response to Gram-positive bacterium
Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKrfNTF
ChainResidueDetails
ACYS39-PHE45

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q9H1E1
ChainResidueDetails
AHIS12
BHIS12

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q9H1E1
ChainResidueDetails
AHIS116
BHIS116

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P15468
ChainResidueDetails
AARG7
BASN43
BTHR44
BPHE117
AHIS12
ALYS40
AASN43
ATHR44
APHE117
BARG7
BHIS12
BLYS40

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:8223579
ChainResidueDetails
AGLN1
BGLN1

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
ALYS40
APHE117
AHIS116
AHIS12

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
BLYS40
BPHE117
BHIS116
BHIS12

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
ALYS40
AHIS116
AHIS12

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
BLYS40
BHIS116
BHIS12

site_idMCSA1
Number of Residues3
DetailsM-CSA 693
ChainResidueDetails
AHIS12proton acceptor, proton donor
ALYS40electrostatic stabiliser
AHIS116proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 693
ChainResidueDetails
BHIS12proton acceptor, proton donor
BLYS40electrostatic stabiliser
BHIS116proton acceptor, proton donor

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PDB entries from 2025-06-11

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