Crystal structure of GltPh in complex with TBOA. Determined by X-ray diffraction at 3.2 Å resolution. Released 27 Feb 2007.
Explore 2NWW in 3D Show helices and sheets RCSB PDB PDBe
2NWW contains 75 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 | 15-31 | 17 | |
| α-helix | 36-39 | 4 | |
| α-helix | 44-67 | 24 | |
| α-helix | 75-79 | 5 | |
| α-helix | 80-106 | 27 | |
| α-helix | 124-129 | 6 | |
| α-helix | 130-134 | 5 | |
| α-helix | 135-137 | 3 | |
| α-helix | 142-147 | 6 | |
| α-helix | 151-168 | 18 | |
| α-helix | 176-201 | 26 | |
| α-helix | 205-219 | 15 | |
| α-helix | 221-223 | 3 | |
| α-helix | 227-242 | 16 | |
| α-helix | 243-247 | 5 | |
| α-helix | 248-252 | 5 | |
| α-helix | 258-275 | 18 | |
| α-helix | 279-281 | 3 | |
| α-helix | 282-290 | 9 | |
| α-helix | 299-302 | 4 | |
| α-helix | 312-329 | 18 | |
| α-helix | 339-350 | 12 | |
| 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 | 15-31 | 17 | |
| α-helix | 36-40 | 5 | |
| α-helix | 44-56 | 13 | |
| α-helix | 58-67 | 10 | |
| α-helix | 75-79 | 5 | |
| α-helix | 80-106 | 27 | |
| α-helix | 124-129 | 6 | |
| α-helix | 131-134 | 4 | |
| α-helix | 142-147 | 6 | |
| α-helix | 151-168 | 18 | |
| α-helix | 176-201 | 26 | |
| α-helix | 205-219 | 15 | |
| α-helix | 221-223 | 3 | |
| α-helix | 227-242 | 16 | |
| α-helix | 243-248 | 6 | |
| α-helix | 249-252 | 4 | |
| α-helix | 258-275 | 18 | |
| α-helix | 282-290 | 9 | |
| α-helix | 296-306 | 11 | |
| α-helix | 312-329 | 18 | |
| α-helix | 339-350 | 12 | |
| 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 | 15-31 | 17 | |
| α-helix | 36-40 | 5 | |
| α-helix | 44-56 | 13 | |
| α-helix | 58-67 | 10 | |
| α-helix | 74-79 | 6 | |
| α-helix | 80-106 | 27 | |
| α-helix | 124-128 | 5 | |
| α-helix | 131-134 | 4 | |
| α-helix | 135-137 | 3 | |
| α-helix | 142-147 | 6 | |
| α-helix | 151-169 | 19 | |
| α-helix | 176-219 | 44 | |
| α-helix | 221-223 | 3 | |
| α-helix | 227-242 | 16 | |
| α-helix | 243-247 | 5 | |
| α-helix | 248-252 | 5 | |
| α-helix | 258-275 | 18 | |
| α-helix | 282-290 | 9 | |
| α-helix | 296-306 | 11 | |
| α-helix | 312-329 | 18 | |
| α-helix | 339-350 | 12 | |
| α-helix | 358-370 | 13 | |
| α-helix | 377-387 | 11 | |
| α-helix | 390-415 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 425aa long hypothetical proton glutamate symport protein | A, B, C | protein | 422 | Pyrococcus horikoshii | O59010 (AlphaFold model) |
>2NWW_1 425aa long hypothetical proton glutamate symport protein (chains A, B, C) MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMP IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS FTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA IMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV PR
| ID | Name | Formula | Copies |
|---|---|---|---|
| TB1 | (3S)-3-(benzyloxy)-L-aspartic acid | C11 H13 N O5 | 3 |
Coupling substrate and ion binding to extracellular gate of a sodium-dependent aspartate transporter. Boudker, O., Ryan, R.M., Yernool, D. et al. Nature (2007) 445:387-393. DOI 10.1038/nature05455 · 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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