2NWX: GltPh

Crystal structure of GltPh in complex with L-aspartate and sodium ions. Determined by X-ray diffraction at 3.29 Å resolution. Released 27 Feb 2007.

Method
X-ray diffraction
Resolution
3.29 Å
Organism
Pyrococcus horikoshii
Chains
3
Atoms
8,596
Mol. weight
135.23 kDa
Ligands
PLM, ASP
Released
27 Feb 2007

Explore 2NWX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2NWX contains 72 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.

Chain A: 24 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix15-3218
α-helix36-427
α-helix44-6825
α-helix74-785
α-helix79-10628
α-helix131-1344
α-helix142-1476
α-helix151-16919
α-helix176-20025
α-helix205-22016
α-helix221-2233
α-helix227-24216
α-helix243-2486
α-helix249-2546
α-helix258-2647
α-helix266-27510
α-helix278-29013
α-helix296-30914
α-helix312-32817
α-helix339-35113
α-helix358-37013
α-helix379-3868
α-helix387-3893
α-helix390-41526
Chain B: 24 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix15-3218
α-helix36-427
α-helix44-6825
α-helix74-785
α-helix79-10628
α-helix131-1344
α-helix135-1373
α-helix142-1476
α-helix151-16919
α-helix176-22045
α-helix221-2233
α-helix227-24216
α-helix243-2486
α-helix249-2546
α-helix258-2647
α-helix266-27510
α-helix278-29013
α-helix299-30911
α-helix312-32817
α-helix339-35113
α-helix358-37013
α-helix379-3868
α-helix387-3893
α-helix390-41526
Chain C: 24 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix15-3218
α-helix36-427
α-helix44-6825
α-helix78-10629
α-helix131-1344
α-helix135-1373
α-helix142-1476
α-helix151-16919
α-helix176-20025
α-helix205-22016
α-helix221-2233
α-helix227-24216
α-helix243-2486
α-helix249-2546
α-helix258-2647
α-helix266-27510
α-helix278-29013
α-helix296-30914
α-helix312-32817
α-helix339-35113
α-helix358-36710
α-helix379-3868
α-helix387-3893
α-helix390-41526

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
425aa long hypothetical proton glutamate symport proteinA, B, Cprotein422Pyrococcus horikoshiiO59010 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>2NWX_1 425aa long hypothetical proton glutamate symport protein (chains A, B, C)
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMP
IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ
QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA
ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS
FTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA
IMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV
PR

Ligands and cofactors

IDNameFormulaCopies
PLMPalmitic acidC16 H32 O23
ASPAspartic acidC4 H7 N O43

Water and common crystallization additives (NA) are not listed.

Primary citation

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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