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3ILQ

Structure of mCD1d with bound glycolipid BbGL-2c from Borrelia burgdorferi

Functional Information from GO Data
ChainGOidnamespacecontents
D0001913biological_processT cell mediated cytotoxicity
D0001916biological_processpositive regulation of T cell mediated cytotoxicity
D0002237biological_processresponse to molecule of bacterial origin
D0002376biological_processimmune system process
D0002474biological_processantigen processing and presentation of peptide antigen via MHC class I
D0002481biological_processantigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent
D0002502biological_processpeptide antigen assembly with MHC class I protein complex
D0002503biological_processpeptide antigen assembly with MHC class II protein complex
D0002726biological_processpositive regulation of T cell cytokine production
D0005198molecular_functionstructural molecule activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005765cellular_componentlysosomal membrane
D0005794cellular_componentGolgi apparatus
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006826biological_processiron ion transport
D0006879biological_processintracellular iron ion homeostasis
D0006955biological_processimmune response
D0006968biological_processcellular defense response
D0007608biological_processsensory perception of smell
D0007611biological_processlearning or memory
D0009897cellular_componentexternal side of plasma membrane
D0010977biological_processnegative regulation of neuron projection development
D0019885biological_processantigen processing and presentation of endogenous peptide antigen via MHC class I
D0019886biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II
D0023026molecular_functionMHC class II protein complex binding
D0030670cellular_componentphagocytic vesicle membrane
D0031902cellular_componentlate endosome membrane
D0033077biological_processT cell differentiation in thymus
D0034756biological_processregulation of iron ion transport
D0042026biological_processprotein refolding
D0042605molecular_functionpeptide antigen binding
D0042612cellular_componentMHC class I protein complex
D0042613cellular_componentMHC class II protein complex
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0042824cellular_componentMHC class I peptide loading complex
D0045646biological_processregulation of erythrocyte differentiation
D0048260biological_processpositive regulation of receptor-mediated endocytosis
D0050680biological_processnegative regulation of epithelial cell proliferation
D0050768biological_processnegative regulation of neurogenesis
D0050778biological_processpositive regulation of immune response
D0050870biological_processpositive regulation of T cell activation
D0051289biological_processprotein homotetramerization
D0060586biological_processmulticellular organismal-level iron ion homeostasis
D0071281biological_processcellular response to iron ion
D0071283biological_processcellular response to iron(III) ion
D0071316biological_processcellular response to nicotine
D1990000biological_processamyloid fibril formation
D1990712cellular_componentHFE-transferrin receptor complex
D2000774biological_processpositive regulation of cellular senescence
D2000978biological_processnegative regulation of forebrain neuron differentiation
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACRVKH
ChainResidueDetails
DTYR78-HIS84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16002697, ECO:0000269|PubMed:16314439, ECO:0000269|PubMed:16537470, ECO:0007744|PDB:1Z5L, ECO:0007744|PDB:2AKR, ECO:0007744|PDB:2FIK
ChainResidueDetails
CASP80

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16002697, ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16314439, ECO:0000269|PubMed:16537470, ECO:0007744|PDB:1Z5L, ECO:0007744|PDB:1ZHN, ECO:0007744|PDB:2AKR, ECO:0007744|PDB:2FIK
ChainResidueDetails
CASP153

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN7
CASN110

site_idSWS_FT_FI4
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16002697, ECO:0000269|PubMed:16007091, ECO:0000269|PubMed:16537470
ChainResidueDetails
CASN20
CASN42
CASN165

218853

PDB entries from 2024-04-24

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