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2BEX

Crystal structure of Placental Ribonuclease Inhibitor in complex with Human Eosinophil Derived Neurotoxin at 2A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006402biological_processmRNA catabolic process
A0008428molecular_functionribonuclease inhibitor activity
A0016477biological_processcell migration
A0030027cellular_componentlamellipodium
A0032311cellular_componentangiogenin-PRI complex
A0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
A0036416biological_processtRNA stabilization
A0045765biological_processregulation of angiogenesis
A0070062cellular_componentextracellular exosome
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006402biological_processmRNA catabolic process
B0008428molecular_functionribonuclease inhibitor activity
B0016477biological_processcell migration
B0030027cellular_componentlamellipodium
B0032311cellular_componentangiogenin-PRI complex
B0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
B0036416biological_processtRNA stabilization
B0045765biological_processregulation of angiogenesis
B0070062cellular_componentextracellular exosome
C0003676molecular_functionnucleic acid binding
D0003676molecular_functionnucleic acid binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MAK B1461
ChainResidue
BTRP263
BGLU264
BHOH2246
DALA99

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A1461
ChainResidue
CASN57
ASER105
ASER106
AARG109
ALEU131
AGLU134

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKnqNTF
ChainResidueDetails
CCYS37-PHE43

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues56
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues54
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues56
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues54
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues56
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues54
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues56
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues54
DetailsRepeat: {"description":"LRR 8"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues56
DetailsRepeat: {"description":"LRR 9"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues54
DetailsRepeat: {"description":"LRR 10"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues56
DetailsRepeat: {"description":"LRR 11"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues54
DetailsRepeat: {"description":"LRR 12"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues56
DetailsRepeat: {"description":"LRR 13"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues54
DetailsRepeat: {"description":"LRR 14"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues56
DetailsRepeat: {"description":"LRR 15"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"PubMed","id":"18694936","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsGlycosylation: {"description":"C-linked (Man) tryptophan","featureId":"CAR_000004","evidences":[{"source":"PubMed","id":"7947762","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9450956","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4y
ChainResidueDetails
CLYS38
CHIS15
CHIS129

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a4y
ChainResidueDetails
DLYS38
DHIS15
DHIS129

242500

PDB entries from 2025-10-01

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