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1Z7X

X-ray structure of human ribonuclease inhibitor complexed with ribonuclease I

Functional Information from GO Data
ChainGOidnamespacecontents
W0005515molecular_functionprotein binding
W0005634cellular_componentnucleus
W0005654cellular_componentnucleoplasm
W0005737cellular_componentcytoplasm
W0005829cellular_componentcytosol
W0005886cellular_componentplasma membrane
W0006402biological_processmRNA catabolic process
W0008428molecular_functionribonuclease inhibitor activity
W0016477biological_processcell migration
W0030027cellular_componentlamellipodium
W0032311cellular_componentangiogenin-PRI complex
W0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
W0036416biological_processtRNA stabilization
W0045765biological_processregulation of angiogenesis
W0070062cellular_componentextracellular exosome
X0003676molecular_functionnucleic acid binding
X0004518molecular_functionnuclease activity
X0004519molecular_functionendonuclease activity
X0004522molecular_functionribonuclease A activity
X0004540molecular_functionRNA nuclease activity
X0005515molecular_functionprotein binding
X0005576cellular_componentextracellular region
X0016787molecular_functionhydrolase activity
X0016829molecular_functionlyase activity
X0050830biological_processdefense response to Gram-positive bacterium
X0051607biological_processdefense response to virus
X0070062cellular_componentextracellular exosome
Y0005515molecular_functionprotein binding
Y0005634cellular_componentnucleus
Y0005654cellular_componentnucleoplasm
Y0005737cellular_componentcytoplasm
Y0005829cellular_componentcytosol
Y0005886cellular_componentplasma membrane
Y0006402biological_processmRNA catabolic process
Y0008428molecular_functionribonuclease inhibitor activity
Y0016477biological_processcell migration
Y0030027cellular_componentlamellipodium
Y0032311cellular_componentangiogenin-PRI complex
Y0034315biological_processregulation of Arp2/3 complex-mediated actin nucleation
Y0036416biological_processtRNA stabilization
Y0045765biological_processregulation of angiogenesis
Y0070062cellular_componentextracellular exosome
Z0003676molecular_functionnucleic acid binding
Z0004518molecular_functionnuclease activity
Z0004519molecular_functionendonuclease activity
Z0004522molecular_functionribonuclease A activity
Z0004540molecular_functionRNA nuclease activity
Z0005515molecular_functionprotein binding
Z0005576cellular_componentextracellular region
Z0016787molecular_functionhydrolase activity
Z0016829molecular_functionlyase activity
Z0050830biological_processdefense response to Gram-positive bacterium
Z0051607biological_processdefense response to virus
Z0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT X 900
ChainResidue
WTYR434
XLYS41
XVAL118
XHIS119
XPHE120
WASP435
WSER460
WHOH519
XARG4
XLYS7
XPHE8
XGLN11
XHIS12

Functional Information from PROSITE/UniProt
site_idPS00127
Number of Residues7
DetailsRNASE_PANCREATIC Pancreatic ribonuclease family signature. CKpvNTF
ChainResidueDetails
XCYS40-PHE46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

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

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; partial","evidences":[{"source":"PubMed","id":"3202829","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"3202829","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues56
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues54
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues56
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues54
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues56
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues54
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues56
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues54
DetailsRepeat: {"description":"LRR 8"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues56
DetailsRepeat: {"description":"LRR 9"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues54
DetailsRepeat: {"description":"LRR 10"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues56
DetailsRepeat: {"description":"LRR 11"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues54
DetailsRepeat: {"description":"LRR 12"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues56
DetailsRepeat: {"description":"LRR 13"}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues54
DetailsRepeat: {"description":"LRR 14"}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues56
DetailsRepeat: {"description":"LRR 15"}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues18
DetailsRegion: {"description":"2 X 5 AA tandem repeats of S-L-D-I-Q"}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
XPHE120
XHIS119
XHIS12
XLYS41

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
ZPHE120
ZHIS119
ZHIS12
ZLYS41

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
XHIS119
XHIS12
XLYS41

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1rbn
ChainResidueDetails
ZHIS119
ZHIS12
ZLYS41

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PDB entries from 2025-12-17

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