Consensus mutated xCT-CD98hc complex. Determined by electron microscopy at 6.2 Å resolution. Released 9 Dec 2020.
Explore 7CCS in 3D Show helices and sheets RCSB PDB PDBe
7CCS contains 49 α-helices and 27 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 168-171 | 4 | |
| α-helix | 177-206 | 30 | |
| β-strand | 225-227 | 3 | 1 |
| α-helix | 231-235 | 5 | |
| α-helix | 242-255 | 14 | |
| β-strand | 259-262 | 4 | 1 |
| β-strand | 266 | 1 | 2 |
| β-strand | 281 | 1 | 2 |
| α-helix | 288-300 | 13 | |
| β-strand | 304-307 | 4 | 1 |
| α-helix | 325-341 | 17 | |
| β-strand | 345-348 | 4 | 3 |
| α-helix | 351-353 | 3 | |
| α-helix | 357-371 | 15 | |
| β-strand | 376-381 | 6 | 3 |
| α-helix | 386-395 | 10 | |
| β-strand | 400-403 | 4 | 3 |
| α-helix | 404-407 | 4 | |
| α-helix | 413-427 | 15 | |
| β-strand | 433-434 | 2 | 4 |
| α-helix | 442-445 | 4 | |
| α-helix | 448-459 | 12 | |
| β-strand | 464-465 | 2 | 4 |
| β-strand | 466-468 | 3 | 1 |
| α-helix | 471-473 | 3 | |
| α-helix | 477-479 | 3 | |
| α-helix | 510-515 | 6 | |
| α-helix | 520-533 | 14 | |
| α-helix | 535-538 | 4 | |
| β-strand | 540-544 | 5 | 5 |
| β-strand | 547 | 1 | 6 |
| β-strand | 551-558 | 8 | 5 |
| β-strand | 563-569 | 7 | 5 |
| β-strand | 576 | 1 | 7 |
| β-strand | 579 | 1 | 6 |
| α-helix | 581-583 | 3 | |
| α-helix | 586-588 | 3 | |
| β-strand | 593-598 | 6 | 5 |
| β-strand | 609-611 | 3 | 5 |
| α-helix | 612-614 | 3 | |
| β-strand | 616 | 1 | 7 |
| β-strand | 621-627 | 7 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 46-54 | 9 | |
| α-helix | 65-70 | 6 | |
| β-strand | 76 | 1 | 8 |
| α-helix | 77-103 | 27 | |
| α-helix | 112-118 | 7 | |
| α-helix | 122-123 | 2 | |
| α-helix | 124-128 | 5 | |
| α-helix | 129-132 | 4 | |
| α-helix | 134-151 | 18 | |
| α-helix | 152-154 | 3 | |
| β-strand | 156 | 1 | 9 |
| β-strand | 158 | 1 | 9 |
| α-helix | 159-161 | 3 | |
| α-helix | 164-181 | 18 | |
| α-helix | 185-201 | 17 | |
| α-helix | 203-215 | 13 | |
| α-helix | 217-220 | 4 | |
| β-strand | 225 | 1 | 8 |
| α-helix | 236-245 | 10 | |
| α-helix | 249-258 | 10 | |
| α-helix | 263-265 | 3 | |
| α-helix | 266-290 | 25 | |
| α-helix | 296-298 | 3 | |
| α-helix | 303-309 | 7 | |
| α-helix | 315-318 | 4 | |
| α-helix | 322-348 | 27 | |
| β-strand | 358-359 | 2 | 10 |
| α-helix | 366-382 | 17 | |
| α-helix | 385-412 | 28 | |
| α-helix | 426-445 | 20 | |
| α-helix | 449-458 | 10 | |
| α-helix | 461-467 | 7 | |
| α-helix | 475-492 | 18 | |
| β-strand | 494-495 | 2 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 4F2 cell-surface antigen heavy chain | A | protein | 631 | Homo sapiens | P08195 (AlphaFold model) |
| Consensus mutated Anionic Amino Acid Transporter Light Chain, Xc- System | B | protein | 509 | Homo sapiens | Q9UPY5 (AlphaFold model) |
>7CCS_1 4F2 cell-surface antigen heavy chain (chains A) GSELQPPEASIAVVSIPRQLPGSHSEAGVQGLSAGDDSELGSHCVAQTGLELLASGDPLP SASQNAEMIETGSDCVTQAGLQLLASSDPPALASKNAEVTGTMSQDTEVDMKEVELNELE PEKQPMNAASGAAMSLAGAEKNGLVKIKVAEDEAEAAAAAKFTGLSKEELLKVAGSPGWV RTRWALLLLFWLGWLGMLAGAVVIIVRAPRCRELPAQKWWHTGALYRIGDLQAFQGHGAG NLAGLKGRLDYLSSLKVKGLVLGPIHKNQKDDVAQTDLLQIDPNFGSKEDFDSLLQSAKK KSIRVILDLTPNYRGENSWFSTQVDTVATKVKDALEFWLQAGVDGFQVRDIENLKDASSF LAEWQNITKGFSEDRLLIAGTNSSDLQQILSLLESNKDLLLTSSYLSDSGSTGEHTKSLV TQYLNATGNRWCSWSLSQARLLTSFLPAQLLRLYQLMLFTLPGTPVFSYGDEIGLDAAAL PGQPMEAPVMLWDESSFPDIPGAVSANMTVKGQSEDPGSLLSLFRRLSDQRSKERSLLHG DFHAFSAGPGLFSYIRHWDQNERFLVVLNFGDVGLSAGLQASDLPASASLPAKADLLLST QPGREEGSPLELERLKLEPHEGLLLRFPYAA
>7CCS_2 Consensus mutated Anionic Amino Acid Transporter Light Chain, Xc- System (chains B) MVRKPVVSTISKGGYLQGNVNGRLPSLGSKEPPGQEKVQLKREITLLDGVSLIVGTIIGA GIFVSPKGVLKNTGSVGLSLVIWAVCGVLSLFGALCYAELGTTIPKSGGAYLYILETFGP LPAFLRGWNELLIIRPASTAVISLAFGNYILEPFFPTCEPPELAIKLLAAVGILLLTVLN SLSVKWSARVQDFFTAAKLLALLIIIVPGVVQLIKGQTQNFKDAFEGSDPSIGGLPLAFY SGLYAYVGWDYLNFVTEEVKNPEKNIPLAIVISMPIVTVAYVLTNVAYFTTLSPEELLLS NAVAVTFGERLLGNFSWAVPIFVALSCFGSLNGSLFAMSRLFYVAAREGHLPKILSMIHV RRHTPLPALIVSGPLTAIMLFLGDLFSLINFMSFGTWLFYGLVVAGLIYLRYKKPDLHRP IKVPLFIPILFLLTCLFLVAVSLYSDPVNCGIGFVIILTGVPVYFLFVYWDKKPKWFRRI SEKITRHLQLLLEVVPEEDKLDYKDDDDK
Consensus mutagenesis approach improves the thermal stability of system x c - transporter, xCT, and enables cryo-EM analyses. Oda, K., Lee, Y., Wiriyasermkul, P. et al. Protein Sci (2020) 29:2398-2407. DOI 10.1002/pro.3966 · PubMed
Other PDB entries of the same protein (UniProt P08195 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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