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1FRT

CRYSTAL STRUCTURE OF THE COMPLEX OF RAT NEONATAL FC RECEPTOR WITH FC

Functional Information from GO Data
ChainGOidnamespacecontents
B0001913biological_processT cell mediated cytotoxicity
B0001916biological_processpositive regulation of T cell mediated cytotoxicity
B0002237biological_processresponse to molecule of bacterial origin
B0002376biological_processimmune system process
B0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
B0002481biological_processantigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent
B0002502biological_processpeptide antigen assembly with MHC class I protein complex
B0002503biological_processpeptide antigen assembly with MHC class II protein complex
B0002726biological_processpositive regulation of T cell cytokine production
B0005198molecular_functionstructural molecule activity
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005765cellular_componentlysosomal membrane
B0006826biological_processiron ion transport
B0006879biological_processintracellular iron ion homeostasis
B0006955biological_processimmune response
B0007608biological_processsensory perception of smell
B0007611biological_processlearning or memory
B0009410biological_processresponse to xenobiotic stimulus
B0009897cellular_componentexternal side of plasma membrane
B0010977biological_processnegative regulation of neuron projection development
B0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
B0019886biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II
B0023026molecular_functionMHC class II protein complex binding
B0031902cellular_componentlate endosome membrane
B0033077biological_processT cell differentiation in thymus
B0034756biological_processregulation of iron ion transport
B0042026biological_processprotein refolding
B0042605molecular_functionpeptide antigen binding
B0042612cellular_componentMHC class I protein complex
B0042613cellular_componentMHC class II protein complex
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042824cellular_componentMHC class I peptide loading complex
B0045646biological_processregulation of erythrocyte differentiation
B0046686biological_processresponse to cadmium ion
B0048260biological_processpositive regulation of receptor-mediated endocytosis
B0050680biological_processnegative regulation of epithelial cell proliferation
B0050768biological_processnegative regulation of neurogenesis
B0050778biological_processpositive regulation of immune response
B0050870biological_processpositive regulation of T cell activation
B0051289biological_processprotein homotetramerization
B0060586biological_processmulticellular organismal-level iron ion homeostasis
B0071281biological_processcellular response to iron ion
B0071283biological_processcellular response to iron(III) ion
B0071316biological_processcellular response to nicotine
B1990000biological_processamyloid fibril formation
B1990712cellular_componentHFE-transferrin receptor complex
B2000774biological_processpositive regulation of cellular senescence
B2000978biological_processnegative regulation of forebrain neuron differentiation
Functional Information from PDB Data
site_idB1A
Number of Residues24
DetailsBINDING SITE FOR FC ON FCRN
ChainResidue
AASN84
AGLU118
APHE119
AGLY131
AGLU132
ATRP133
APRO134
AGLU135
ATHR136
AASP137
BILE1
AGLN85
BGLN2
BLYS3
BTHR4
BTHR86
BLYS88
AILE86
APHE90
AALA113
ALEU114
AASN115
AGLY116
AGLU117

site_idB1B
Number of Residues25
DetailsBINDING SITE FOR FCRN ON FC
ChainResidue
CLYS248
CTHR250
CLEU251
CMET252
CILE253
CSER254
CARG255
CTHR256
CPRO257
CLYS288
CLYS290
CPRO291
CVAL308
CLEU309
CHIS310
CGLN311
CLEU314
CGLY385
CGLN386
CPRO387
CMET428
CHIS433
CASN434
CHIS435
CTYR436

site_idB2A
Number of Residues2
DetailsPOSSIBLE BINDING SITE FOR FC ON THE SECOND MOLECULE OF THE FCRN DIMER
ChainResidue
ALEU219
ALYS245

site_idB2B
Number of Residues2
DetailsPOSSIBLE BINDING SITE FOR FCRN ASSUMING THE PRESENCE OF THE FCRN DIMER
ChainResidue
CGLN272
CHIS285

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVKH
ChainResidueDetails
BTYR78-HIS84
ATYR252-HIS258
CPHE423-HIS429

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN87
AASN104
AASN128
AASN225

218196

PDB entries from 2024-04-10

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