2NWW: GltPh

Crystal structure of GltPh in complex with TBOA. Determined by X-ray diffraction at 3.2 Å resolution. Released 27 Feb 2007.

Method
X-ray diffraction
Resolution
3.2 Å
Organism
Pyrococcus horikoshii
Chains
3
Atoms
8,772
Mol. weight
134.64 kDa
Ligands
TB1
Released
27 Feb 2007

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

Secondary structure: helices and β-sheets

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.

Chain A: 26 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix15-3117
α-helix36-394
α-helix44-6724
α-helix75-795
α-helix80-10627
α-helix124-1296
α-helix130-1345
α-helix135-1373
α-helix142-1476
α-helix151-16818
α-helix176-20126
α-helix205-21915
α-helix221-2233
α-helix227-24216
α-helix243-2475
α-helix248-2525
α-helix258-27518
α-helix279-2813
α-helix282-2909
α-helix299-3024
α-helix312-32918
α-helix339-35012
α-helix358-37013
α-helix377-38610
α-helix387-3893
α-helix390-41526
Chain B: 25 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix15-3117
α-helix36-405
α-helix44-5613
α-helix58-6710
α-helix75-795
α-helix80-10627
α-helix124-1296
α-helix131-1344
α-helix142-1476
α-helix151-16818
α-helix176-20126
α-helix205-21915
α-helix221-2233
α-helix227-24216
α-helix243-2486
α-helix249-2524
α-helix258-27518
α-helix282-2909
α-helix296-30611
α-helix312-32918
α-helix339-35012
α-helix358-37013
α-helix377-38610
α-helix387-3893
α-helix390-41526
Chain C: 24 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix15-3117
α-helix36-405
α-helix44-5613
α-helix58-6710
α-helix74-796
α-helix80-10627
α-helix124-1285
α-helix131-1344
α-helix135-1373
α-helix142-1476
α-helix151-16919
α-helix176-21944
α-helix221-2233
α-helix227-24216
α-helix243-2475
α-helix248-2525
α-helix258-27518
α-helix282-2909
α-helix296-30611
α-helix312-32918
α-helix339-35012
α-helix358-37013
α-helix377-38711
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
>2NWW_1 425aa long hypothetical proton glutamate symport protein (chains A, B, C)
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMP
IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ
QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA
ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS
FTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA
IMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV
PR

Ligands and cofactors

IDNameFormulaCopies
TB1(3S)-3-(benzyloxy)-L-aspartic acidC11 H13 N O53

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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