2NWL: GltPh

Crystal structure of GltPh in complex with L-Asp. Determined by X-ray diffraction at 2.96 Å resolution. Released 27 Feb 2007.

Method: X-ray diffraction
Resolution: 2.96 Å
Organism: Pyrococcus horikoshii
Chains: 3
Atoms: 8,656
Mol. weight: 135.05 kDa
Ligands: ASP, PLM
Released: 27 Feb 2007

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

Secondary structure: helices and β-sheets

2NWL contains 68 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: 23 helices, 0 β-strands

Element	Residues	Length
α-helix	15-32	18
α-helix	36-42	7
α-helix	44-69	26
α-helix	74-78	5
α-helix	79-106	28
α-helix	131-134	4
α-helix	135-137	3
α-helix	142-147	6
α-helix	151-169	19
α-helix	174-201	28
α-helix	205-217	13
α-helix	221-223	3
α-helix	227-242	16
α-helix	243-248	6
α-helix	249-253	5
α-helix	258-275	18
α-helix	278-290	13
α-helix	296-306	11
α-helix	312-329	18
α-helix	339-351	13
α-helix	358-370	13
α-helix	379-387	9
α-helix	390-415	26

Chain B: 22 helices, 0 β-strands

Element	Residues	Length
α-helix	15-32	18
α-helix	36-42	7
α-helix	44-69	26
α-helix	78-106	29
α-helix	131-134	4
α-helix	135-137	3
α-helix	142-147	6
α-helix	151-169	19
α-helix	174-201	28
α-helix	205-217	13
α-helix	221-223	3
α-helix	227-242	16
α-helix	243-248	6
α-helix	249-253	5
α-helix	258-275	18
α-helix	282-290	9
α-helix	296-309	14
α-helix	312-329	18
α-helix	339-351	13
α-helix	358-369	12
α-helix	377-387	11
α-helix	390-415	26

Chain C: 23 helices, 0 β-strands

Element	Residues	Length
α-helix	15-32	18
α-helix	36-42	7
α-helix	44-69	26
α-helix	74-78	5
α-helix	79-106	28
α-helix	131-134	4
α-helix	135-137	3
α-helix	142-147	6
α-helix	151-168	18
α-helix	174-201	28
α-helix	205-217	13
α-helix	221-223	3
α-helix	227-242	16
α-helix	243-247	5
α-helix	248-253	6
α-helix	258-275	18
α-helix	282-290	9
α-helix	296-309	14
α-helix	312-329	18
α-helix	339-351	13
α-helix	358-369	12
α-helix	379-387	9
α-helix	390-415	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
glutamate symport protein	A, B, C	protein	422	Pyrococcus horikoshii	O59010 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>2NWL_1 glutamate symport protein (chains A, B, C)
MGLYRKYIEYPVLIKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMP
IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ
QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA
ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS
FTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA
IMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV
PR

Ligands and cofactors

ID	Name	Formula	Copies
ASP	Aspartic acid	C4 H7 N O4	3
PLM	Palmitic acid	C16 H32 O2	3

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:

7RCP 2.2 Å, GltPh mutant (S279E/D405N) in complex with aspartate and sodium ions
7AHK 2.5 Å, Crystal structure of the outward-facing state of the substrate-free Na+-only bound…
7UG0 2.55 Å, TBOA-bound GltPh RSMR mutant in IFS state
9BH2 2.7 Å, Apo GltPh, outward-facing state
7UGJ 2.81 Å, TBOA-bound GltPh RSMR mutant in OFS state
7UGV 2.94 Å, Asp-bound GltPh RSMR mutant in IFS-A2 state
7UGD 2.95 Å, Asp-bound GltPh RSMR mutant in IFS-A1 state
7UGX 2.96 Å, Asp-bound GltPh RSMR mutant in IFS-B1 state
7UH3 2.99 Å, Asp-bound GltPh RSMR mutant in iOFS state
6X15 3.05 Å, Inward-facing state of the glutamate transporter homologue GltPh in complex with…
6UWF 3.08 Å, GltPh in complex with L-aspartate and sodium ions in outward-facing state
9BH1 3.1 Å, Apo GltPh, intermediate outward-facing state

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