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1IFA

THREE-DIMENSIONAL CRYSTAL STRUCTURE OF RECOMBINANT MURINE INTERFERON-BETA

Functional Information from GO Data
ChainGOidnamespacecontents
A0002250biological_processadaptive immune response
A0002286biological_processT cell activation involved in immune response
A0002312biological_processB cell activation involved in immune response
A0002323biological_processnatural killer cell activation involved in immune response
A0002683biological_processnegative regulation of immune system process
A0005125molecular_functioncytokine activity
A0005126molecular_functioncytokine receptor binding
A0005132molecular_functiontype I interferon receptor binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0006952biological_processdefense response
A0006955biological_processimmune response
A0006959biological_processhumoral immune response
A0007165biological_processsignal transduction
A0009893biological_processpositive regulation of metabolic process
A0010508biological_processpositive regulation of autophagy
A0042100biological_processB cell proliferation
A0042742biological_processdefense response to bacterium
A0043330biological_processresponse to exogenous dsRNA
A0045321biological_processleukocyte activation
A0045671biological_processnegative regulation of osteoclast differentiation
A0051241biological_processnegative regulation of multicellular organismal process
A0051607biological_processdefense response to virus
A0060337biological_processtype I interferon-mediated signaling pathway
A0070050biological_processneuron cellular homeostasis
A0071359biological_processcellular response to dsRNA
A0071549biological_processcellular response to dexamethasone stimulus
A0098586biological_processcellular response to virus
A0140123biological_processnegative regulation of Lewy body formation
Functional Information from PROSITE/UniProt
site_idPS00252
Number of Residues19
DetailsINTERFERON_A_B_D Interferon alpha, beta and delta family signature. YYwRVqrYLklmkynsYAW
ChainResidueDetails
ATYR120-TRP138

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P70499
ChainResidueDetails
ATYR3

site_idSWS_FT_FI2
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:3360010
ChainResidueDetails
AASN29
AASN69
AASN76

238268

PDB entries from 2025-07-02

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