Apo GltPh, outward-facing state. Determined by electron microscopy at 2.7 Å resolution. Released 12 Mar 2025.
Explore 9BH2 in 3D Show helices and sheets RCSB PDB PDBe
9BH2 contains 24 α-helices and 0 β-strands across 1 chain. 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 | 4-9 | 6 | |
| α-helix | 12-33 | 22 | |
| α-helix | 36-38 | 3 | |
| α-helix | 39-43 | 5 | |
| α-helix | 44-72 | 29 | |
| α-helix | 75-107 | 33 | |
| α-helix | 127-129 | 3 | |
| α-helix | 130-136 | 7 | |
| α-helix | 142-147 | 6 | |
| α-helix | 151-169 | 19 | |
| α-helix | 174-220 | 47 | |
| α-helix | 221-223 | 3 | |
| α-helix | 227-241 | 15 | |
| α-helix | 242-247 | 6 | |
| α-helix | 248-253 | 6 | |
| α-helix | 258-275 | 18 | |
| α-helix | 282-291 | 10 | |
| α-helix | 296-309 | 14 | |
| α-helix | 312-329 | 18 | |
| α-helix | 337-347 | 11 | |
| α-helix | 348-352 | 5 | |
| α-helix | 358-370 | 13 | |
| α-helix | 377-387 | 11 | |
| α-helix | 390-415 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glutamate transporter homolog | A | protein | 422 | Pyrococcus horikoshii | O59010 (AlphaFold model) |
>9BH2_1 Glutamate transporter homolog (chains A) MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMP IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS FTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA IMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV PR
Evolutionary analysis reveals the origin of sodium coupling in glutamate transporters. Reddy, K.D., Rasool, B., Akher, F.B. et al. bioRxiv (2024). DOI 10.1101/2023.12.03.569786 · 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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