Crystal Structure of Wild-Type GltPh in complex with L-aspartate. Determined by X-ray diffraction at 3.4 Å resolution. Released 17 Jan 2018.
Explore 6BAT in 3D Show helices and sheets RCSB PDB PDBe
6BAT contains 69 α-helices and 0 β-strands across 3 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 | 12-32 | 21 | |
| α-helix | 36-42 | 7 | |
| α-helix | 44-72 | 29 | |
| α-helix | 75-106 | 32 | |
| α-helix | 127-129 | 3 | |
| α-helix | 130-135 | 6 | |
| α-helix | 142-147 | 6 | |
| α-helix | 151-169 | 19 | |
| α-helix | 175-201 | 27 | |
| α-helix | 205-220 | 16 | |
| α-helix | 226-242 | 17 | |
| α-helix | 243-248 | 6 | |
| α-helix | 249-254 | 6 | |
| α-helix | 258-264 | 7 | |
| α-helix | 266-275 | 10 | |
| α-helix | 282-291 | 10 | |
| α-helix | 296-309 | 14 | |
| α-helix | 312-329 | 18 | |
| α-helix | 331-334 | 4 | |
| α-helix | 335-351 | 17 | |
| α-helix | 358-370 | 13 | |
| α-helix | 379-386 | 8 | |
| α-helix | 390-415 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-32 | 21 | |
| α-helix | 36-42 | 7 | |
| α-helix | 44-72 | 29 | |
| α-helix | 75-106 | 32 | |
| α-helix | 124-129 | 6 | |
| α-helix | 130-135 | 6 | |
| α-helix | 142-147 | 6 | |
| α-helix | 151-169 | 19 | |
| α-helix | 175-203 | 29 | |
| α-helix | 205-220 | 16 | |
| α-helix | 221-223 | 3 | |
| α-helix | 227-242 | 16 | |
| α-helix | 243-248 | 6 | |
| α-helix | 249-253 | 5 | |
| α-helix | 258-264 | 7 | |
| α-helix | 266-275 | 10 | |
| α-helix | 278-291 | 14 | |
| α-helix | 296-308 | 13 | |
| α-helix | 312-327 | 16 | |
| α-helix | 338-351 | 14 | |
| α-helix | 358-370 | 13 | |
| α-helix | 377-386 | 10 | |
| α-helix | 387-389 | 3 | |
| α-helix | 390-415 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-32 | 21 | |
| α-helix | 36-42 | 7 | |
| α-helix | 44-72 | 29 | |
| α-helix | 75-106 | 32 | |
| α-helix | 126-129 | 4 | |
| α-helix | 130-135 | 6 | |
| α-helix | 142-147 | 6 | |
| α-helix | 151-169 | 19 | |
| α-helix | 175-220 | 46 | |
| α-helix | 227-242 | 16 | |
| α-helix | 243-247 | 5 | |
| α-helix | 248-253 | 6 | |
| α-helix | 258-264 | 7 | |
| α-helix | 266-275 | 10 | |
| α-helix | 282-291 | 10 | |
| α-helix | 296-306 | 11 | |
| α-helix | 312-328 | 17 | |
| α-helix | 335-351 | 17 | |
| α-helix | 359-363 | 5 | |
| α-helix | 365-368 | 4 | |
| α-helix | 377-387 | 11 | |
| α-helix | 390-415 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate transporter homolog | A, B, C | protein | 420 | Pyrococcus horikoshii | O59010 (AlphaFold model) |
>6BAT_1 Glutamate transporter homolog (chains A, B, C) MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYADAVKTYVKPFGDLFVRLLKMLVMP IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ QFQPKQAPPLVKILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVKVVGELAKVTAAVYVGLT LQILLVYFVLLKIYGIDPISFIKKAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS FTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA IMLAMVLESVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV
| ID | Name | Formula | Copies |
|---|---|---|---|
| ASP | Aspartic acid | C4 H7 N O4 | 3 |
Water and common crystallization additives (NA) are not listed.
Structural characterisation reveals insights into substrate recognition by the glutamine transporter ASCT2/SLC1A5. Scopelliti, A.J., Font, J., Vandenberg, R.J. et al. Nat Commun (2018) 9:38-38. DOI 10.1038/s41467-017-02444-w · PubMed
Other PDB entries of the same protein (UniProt O59010 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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