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1DYT

X-ray crystal structure of ECP (RNase 3) at 1.75 A

Functional Information from GO Data
ChainGOidnamespacecontents
A0001530molecular_functionlipopolysaccharide binding
A0002227biological_processinnate immune response in mucosa
A0003676molecular_functionnucleic acid binding
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004540molecular_functionRNA nuclease activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006401biological_processRNA catabolic process
A0006935biological_processchemotaxis
A0016787molecular_functionhydrolase activity
A0019731biological_processantibacterial humoral response
A0035578cellular_componentazurophil granule lumen
A0042742biological_processdefense response to bacterium
A0043152biological_processinduction of bacterial agglutination
A0045087biological_processinnate immune response
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
B0001530molecular_functionlipopolysaccharide binding
B0002227biological_processinnate immune response in mucosa
B0003676molecular_functionnucleic acid binding
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004540molecular_functionRNA nuclease activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0006401biological_processRNA catabolic process
B0006935biological_processchemotaxis
B0016787molecular_functionhydrolase activity
B0019731biological_processantibacterial humoral response
B0035578cellular_componentazurophil granule lumen
B0042742biological_processdefense response to bacterium
B0043152biological_processinduction of bacterial agglutination
B0045087biological_processinnate immune response
B0050829biological_processdefense response to Gram-negative bacterium
B0050830biological_processdefense response to Gram-positive bacterium
B0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE B 300
ChainResidue
BARG34
BCIT302
BHOH2144

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE FE A 300
ChainResidue
ACIT302

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT A 301
ChainResidue
APHE76
AVAL78
ATYR107
AHOH2109
AHOH2180
AHOH2181
AHOH2182
BARG121
ATHR46
AASN50
AVAL54
ASER74
AARG75

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT B 301
ChainResidue
AARG61
AARG66
BTHR46
BASN50
BVAL54
BSER74
BARG75
BPHE76
BVAL78
BTYR107
BHOH2083
BHOH2142
BHOH2143

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE CIT A 302
ChainResidue
AARG34
ALYS38
AASN39
AGLN40
AFE300
AHOH2094
AHOH2096
AHOH2183
AHOH2184
AHOH2185

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE CIT B 302
ChainResidue
BARG34
BARG36
BCYS37
BLYS38
BASN39
BGLN40
BFE300
BHOH2068
BHOH2144
BHOH2145
BHOH2146
BHOH2147

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKnqNTF
ChainResidueDetails
ACYS37-PHE43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues88
DetailsRegion: {"description":"Required for nearly all of the bactericidal activity; partially involved in LPS-binding and bacterial membrane depolarization"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"May be involved in LPS-binding"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"May be involved in LPS- and LTA-binding"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"PubMed","id":"18694936","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues6
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
AHIS128

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4y
ChainResidueDetails
BLYS38
BHIS15
BHIS128

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PDB entries from 2025-07-30

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