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2RNF

X-RAY CRYSTAL STRUCTURE OF HUMAN RIBONUCLEASE 4 IN COMPLEX WITH D(UP)

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 PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE UM3 A 301
ChainResidue
AARG7
AGLY119
AHOH333
AGLN11
AHIS12
ALYS40
APHE42
AASN43
ATHR44
AARG101
APHE117

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE UM3 B 302
ChainResidue
BHIS12
BPHE42
BASN43
BTHR44
BARG101
BPHE117
BGLY119

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9H1E1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q9H1E1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P15468","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PubMed","id":"8223579","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 9878400
ChainResidueDetails
ALYS40
AHIS116

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 2025-10-29

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