6UWF: GltPh

GltPh in complex with L-aspartate and sodium ions in outward-facing state. Determined by electron microscopy at 3.08 Å resolution. Released 3 Jun 2020.

Method: Electron microscopy
Resolution: 3.08 Å
Organism: Pyrococcus horikoshii
Chains: 1
Atoms: 3,178
Mol. weight: 46.24 kDa
Ligands: ASP, 6OU
Released: 3 Jun 2020

Explore 6UWF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6UWF contains 22 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.

Chain A: 22 helices, 0 β-strands

Element	Residues	Length
α-helix	3-8	6
α-helix	12-32	21
α-helix	36-38	3
α-helix	39-43	5
α-helix	45-56	12
α-helix	58-68	11
α-helix	76-106	31
α-helix	131-135	5
α-helix	142-147	6
α-helix	151-168	18
α-helix	174-220	47
α-helix	227-242	16
α-helix	243-247	5
α-helix	248-252	5
α-helix	258-275	18
α-helix	282-291	10
α-helix	296-306	11
α-helix	312-328	17
α-helix	335-351	17
α-helix	358-370	13
α-helix	377-388	12
α-helix	390-415	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glutamate transporter homolog	A	protein	422	Pyrococcus horikoshii	O59010 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6UWF_1 Glutamate transporter homolog (chains A)
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMP
IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ
QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA
ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS
FTLPLGATINMDGTALYQGVCTFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA
IMLAMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV
PR

Ligands and cofactors

ID	Name	Formula	Copies
ASP	Aspartic acid	C4 H7 N O4	1
6OU	[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-y…	C39 H76 N O8 P	2

Primary citation

Use of paramagnetic 19 F NMR to monitor domain movement in a glutamate transporter homolog. Huang, Y., Wang, X., Lv, G. et al. Nat Chem Biol (2020) 16:1006-1012. DOI 10.1038/s41589-020-0561-6 · 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
2NWL 2.96 Å, Crystal structure of GltPh in complex with L-Asp
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…
9BH1 3.1 Å, Apo GltPh, intermediate outward-facing state

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