Structure of glutamate transporter homolog from Pyrococcus horikoshii. Determined by X-ray diffraction at 3.5 Å resolution. Released 26 Oct 2004.
Explore 1XFH in 3D Show helices and sheets RCSB PDB PDBe
1XFH contains 79 α-helices and 6 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 | 13-33 | 21 | |
| α-helix | 36-42 | 7 | |
| α-helix | 46-55 | 10 | |
| α-helix | 58-67 | 10 | |
| α-helix | 74-78 | 5 | |
| α-helix | 79-106 | 28 | |
| α-helix | 131-134 | 4 | |
| α-helix | 135-137 | 3 | |
| α-helix | 142-146 | 5 | |
| β-strand | 147 | 1 | 1 |
| β-strand | 149 | 1 | 1 |
| α-helix | 153-169 | 17 | |
| α-helix | 175-200 | 26 | |
| α-helix | 205-220 | 16 | |
| α-helix | 221-223 | 3 | |
| α-helix | 226-242 | 17 | |
| α-helix | 243-248 | 6 | |
| α-helix | 249-252 | 4 | |
| α-helix | 258-264 | 7 | |
| α-helix | 266-275 | 10 | |
| α-helix | 278-290 | 13 | |
| α-helix | 299-302 | 4 | |
| α-helix | 304-306 | 3 | |
| α-helix | 312-328 | 17 | |
| α-helix | 339-351 | 13 | |
| α-helix | 364-370 | 7 | |
| α-helix | 379-386 | 8 | |
| α-helix | 390-397 | 8 | |
| α-helix | 400-414 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-31 | 19 | |
| α-helix | 36-42 | 7 | |
| α-helix | 44-55 | 12 | |
| α-helix | 58-67 | 10 | |
| α-helix | 74-78 | 5 | |
| α-helix | 79-106 | 28 | |
| α-helix | 131-134 | 4 | |
| α-helix | 135-137 | 3 | |
| α-helix | 142-146 | 5 | |
| β-strand | 147 | 1 | 2 |
| β-strand | 149 | 1 | 2 |
| α-helix | 153-169 | 17 | |
| α-helix | 174-200 | 27 | |
| α-helix | 205-220 | 16 | |
| α-helix | 221-223 | 3 | |
| α-helix | 228-241 | 14 | |
| α-helix | 242-248 | 7 | |
| α-helix | 249-252 | 4 | |
| α-helix | 258-264 | 7 | |
| α-helix | 266-275 | 10 | |
| α-helix | 278-290 | 13 | |
| α-helix | 299-306 | 8 | |
| α-helix | 312-327 | 16 | |
| α-helix | 339-351 | 13 | |
| α-helix | 363-370 | 8 | |
| α-helix | 377-386 | 10 | |
| α-helix | 390-415 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-32 | 20 | |
| α-helix | 36-40 | 5 | |
| α-helix | 44-67 | 24 | |
| α-helix | 74-78 | 5 | |
| α-helix | 79-106 | 28 | |
| α-helix | 113-114 | 2 | |
| α-helix | 131-134 | 4 | |
| α-helix | 135-137 | 3 | |
| α-helix | 142-146 | 5 | |
| β-strand | 147 | 1 | 3 |
| β-strand | 149 | 1 | 3 |
| α-helix | 153-169 | 17 | |
| α-helix | 174-200 | 27 | |
| α-helix | 205-216 | 12 | |
| α-helix | 217-221 | 5 | |
| α-helix | 226-241 | 16 | |
| α-helix | 242-248 | 7 | |
| α-helix | 249-253 | 5 | |
| α-helix | 258-264 | 7 | |
| α-helix | 266-274 | 9 | |
| α-helix | 278-290 | 13 | |
| α-helix | 299-306 | 8 | |
| α-helix | 312-327 | 16 | |
| α-helix | 339-351 | 13 | |
| α-helix | 361-363 | 3 | |
| α-helix | 364-370 | 7 | |
| α-helix | 378-386 | 9 | |
| α-helix | 387-389 | 3 | |
| α-helix | 390-415 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| proton glutamate symport protein | A, B, C | protein | 422 | Pyrococcus horikoshii | O59010 (AlphaFold model) |
>1XFH_1 proton glutamate symport protein (chains A, B, C) MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMP IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS FTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA IMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV PR
Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Yernool, D., Boudker, O., Jin, Y. et al. Nature (2004) 431:811-818. DOI 10.1038/nature03018 · PubMed
Other PDB entries of the same protein (UniProt O59010 (AlphaFold model), which also has an AlphaFold model), best resolution first:
1XFH is part of these collections:
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