eF-site ID 6i9q-A PDB Code 6i9q Chain A click to enlarge Title Structure of the mouse CD98 heavy chain ectodomain Classification MEMBRANE PROTEIN Compound 4F2 cell-surface antigen heavy chain Source (4F2_MOUSE) Sequence A:  ELPVQRWWHKGALYRIGDLQAFVGRDAGGIAGLKSHLEYL STLKVKGLVLGPIHKNQKDEINETDLKQINPTLGSQEDFK DLLQSAKKKSIHIILDLTPNYQGQNAWFLPAQADIVATKM KEALSSWLQDGVDGFQFRDVGKLMNAPLYLAEWQNITKNL SEDRLLIAGTESSDLQQIVNILESTSDLLLTSSYLSNSTF TGERTESLVTRFLNATGSQWCSWSVSQAGLLADFIPDHLL RLYQLLLFTLPGTPVFSYGDELGLQGALPGQPAKAPLMPW NESSIFHIPRPVSLNMTVKGQNEDPGSLLTQFRRLSDLRG KERSLLHGDFHALSSSPDLFSYIRHWDQNERYLVVLNFRD SGRSARLGASNLPAGISLPASAKLLLSTDSARQSREEDTS LKLENLSLNPYEGLLLQFPFVA Description Functional site 1) chain A residue 316 type sequence F description binding site for residue EDO A 601 source : AC1 2) chain A residue 326 type sequence S description binding site for residue EDO A 601 source : AC1 3) chain A residue 327 type sequence W description binding site for residue EDO A 601 source : AC1 4) chain A residue 328 type sequence S description binding site for residue EDO A 601 source : AC1 5) chain A residue 492 type sequence T description binding site for residue EDO A 602 source : AC2 6) chain A residue 493 type sequence D description binding site for residue EDO A 602 source : AC2 7) chain A residue 515 type sequence Y description binding site for residue EDO A 602 source : AC2 8) chain A residue 243 type sequence D description binding site for residue CL A 603 source : AC3 9) chain A residue 244 type sequence V description binding site for residue CL A 603 source : AC3 10) chain A residue 245 type sequence G description binding site for residue CL A 603 source : AC3 11) chain A residue 274 type sequence T description binding site for residue CL A 603 source : AC3 12) chain A residue 275 type sequence E description binding site for residue CL A 603 source : AC3 13) chain A residue 300 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P08195 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 302 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P08195 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 420 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P08195 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 166 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 259 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 385 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 399 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 318 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P08195 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 263 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 301 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 509 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI3

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