7UH3: Asp-bound GltPh RSMR mutant in iOFS state

Asp-bound GltPh RSMR mutant in iOFS state. Determined by electron microscopy at 2.99 Å resolution. Released 29 Mar 2023.

Method: Electron microscopy
Resolution: 2.99 Å
Organism: Pyrococcus horikoshii
Chains: 1
Atoms: 3,096
Mol. weight: 44.34 kDa
Ligands: ASP
Released: 29 Mar 2023

Explore 7UH3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7UH3 contains 26 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: 26 helices, 0 β-strands

Element	Residues	Length
α-helix	3-9	7
α-helix	12-32	21
α-helix	36-38	3
α-helix	39-43	5
α-helix	44-71	28
α-helix	75-106	32
α-helix	124-129	6
α-helix	130-135	6
α-helix	142-147	6
α-helix	152-168	17
α-helix	174-216	43
α-helix	217-221	5
α-helix	223-226	4
α-helix	229-235	7
α-helix	236-242	7
α-helix	243-254	12
α-helix	258-264	7
α-helix	266-275	10
α-helix	282-292	11
α-helix	296-309	14
α-helix	312-329	18
α-helix	335-351	17
α-helix	358-362	5
α-helix	364-370	7
α-helix	377-386	10
α-helix	390-415	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glutamate transporter homolog	A	protein	418	Pyrococcus horikoshii	O59010 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7UH3_1 Glutamate transporter homolog (chains A)
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLKMLVMP
IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ
QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA
ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAHVMAHQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTSSSSGTLPVTMRVAKEMGISEGIYS
FTLPLGATINMDGTALYQGVATFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA
IMLAMVLHSVGLPLTDPNVAAAYACILGIDAILDRGRTMVNVTGDLTGTAIVAKTEGT

Ligands and cofactors

ID	Name	Formula	Copies
ASP	Aspartic acid	C4 H7 N O4	1

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

Primary citation

Environmentally Ultrasensitive Fluorine Probe to Resolve Protein Conformational Ensembles by 19F NMR and Cryo-EM. Huang, Y., Reddy, K.D., Bracken, C. et al. J Am Chem Soc (2023) 145:8583-8592. DOI 10.1021/jacs.3c01003

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
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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