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1GQV

Atomic Resolution (0.98A) Structure of Eosinophil-Derived Neurotoxin

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
A0004522molecular_functionribonuclease A activity
A0004540molecular_functionRNA nuclease activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0006401biological_processRNA catabolic process
A0006935biological_processchemotaxis
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0035578cellular_componentazurophil granule lumen
A0043152biological_processinduction of bacterial agglutination
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A0051607biological_processdefense response to virus
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 135
ChainResidue
ATHR46
AASN50
AVAL78
ATYR107
AHOH2225
AHOH2226

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 Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS15

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS129

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS38

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: 3'-nitrotyrosine => ECO:0000269|PubMed:18694936
ChainResidueDetails
ATYR33

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: C-linked (Man) tryptophan => ECO:0000269|PubMed:7947762, ECO:0000269|PubMed:9450956
ChainResidueDetails
ATRP7

site_idSWS_FT_FI6
Number of Residues5
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN17
AASN59
AASN65
AASN84
AASN92

217705

PDB entries from 2024-03-27

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