4P19: PDB entry 4P19

Closed, apo inward-facing state of the glutamate transporter homologue GltPh. Determined by X-ray diffraction at 3.25 Å resolution. Released 4 Jun 2014.

Method: X-ray diffraction
Resolution: 3.25 Å
Organism: Pyrococcus horikoshii
Chains: 3
Atoms: 9,124
Mol. weight: 134.45 kDa
Ligands: HG
Released: 4 Jun 2014

Explore 4P19 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4P19 contains 56 α-helices and 1 β-strand 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: 18 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	12-32	21
α-helix	36-42	7
α-helix	44-73	30
α-helix	80-106	27
β-strand	109-112	4	1
α-helix	130-135	6
α-helix	142-147	6
α-helix	151-168	18
α-helix	174-220	47
α-helix	223-242	20
α-helix	243-248	6
α-helix	249-252	4
α-helix	258-275	18
α-helix	278-291	14
α-helix	296-309	14
α-helix	312-328	17
α-helix	335-349	15
α-helix	358-369	12
α-helix	377-414	38

Chain B: 19 helices, 0 β-strands

Element	Residues	Length
α-helix	12-32	21
α-helix	36-38	3
α-helix	39-43	5
α-helix	44-73	30
α-helix	80-106	27
α-helix	130-135	6
α-helix	142-147	6
α-helix	151-168	18
α-helix	174-220	47
α-helix	223-242	20
α-helix	243-248	6
α-helix	249-253	5
α-helix	258-275	18
α-helix	282-291	10
α-helix	296-309	14
α-helix	312-328	17
α-helix	335-346	12
α-helix	358-367	10
α-helix	377-414	38

Chain C: 19 helices, 0 β-strands

Element	Residues	Length
α-helix	12-32	21
α-helix	36-38	3
α-helix	39-43	5
α-helix	44-73	30
α-helix	80-106	27
α-helix	130-135	6
α-helix	142-147	6
α-helix	151-168	18
α-helix	174-220	47
α-helix	223-242	20
α-helix	243-247	5
α-helix	248-252	5
α-helix	258-275	18
α-helix	278-291	14
α-helix	296-309	14
α-helix	312-329	18
α-helix	335-348	14
α-helix	358-370	13
α-helix	377-414	38

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
425aa long hypothetical proton glutamate symport protein	A, B, C	protein	422	Pyrococcus horikoshii	O59010 (AlphaFold model)

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

>4P19_1 425aa long hypothetical proton glutamate symport protein (chains A, B, C)
MGLYRKYIEYPVLQKILIGLILGAIVGLILGHYGYAHAVHTYVKPFGDLFVRLLCMLVMP
IVFASLVVGAASISPARLGRVGVKIVVYYLLTSAFAVTLGIIMARLFNPGAGIHLAVGGQ
QFQPHQAPPLVHILLDIVPTNPFGALANGQVLPTIFFAIILGIAITYLMNSENEKVRKSA
ETLLDAINGLAEAMYKIVNGVMQYAPIGVFALIAYVMAEQGVHVVGELAKVTAAVYVGLT
LQILLVYFVLLKIYGIDPISFIKHAKDAMLTAFVTRSSSGTLPVTMRVAKEMGISEGIYS
FTLPLGATINMDGTALYQGVATFFIANALGSHLTVGQQLTIVLTAVLASIGTAGVPGAGA
IMLCMVLHSVGLPLTDPNVAAAYAMILGIDAILDMGRTMVNVTGDLTGTAIVAKTEGTLV
PR

Ligands and cofactors

ID	Name	Formula	Copies
HG	Mercury (II) ion	Hg	3

Primary citation

Coupled ion binding and structural transitions along the transport cycle of glutamate transporters. Verdon, G., Oh, S., Serio, R.N. et al. Elife (2014) 3:e02283-e02283. DOI 10.7554/eLife.02283 · 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…
6UWF 3.08 Å, GltPh in complex with L-aspartate and sodium ions in outward-facing state

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