4ATV: Na/h antiporter nhaa

Structure of a triple mutant of the nhaa dimer, crystallised at low PH. Determined by X-ray diffraction at 3.5 Å resolution. Released 10 Jul 2013.

Method: X-ray diffraction
Resolution: 3.5 Å
Organism: ESCHERICHIA COLI
Chains: 4
Atoms: 11,331
Mol. weight: 174.88 kDa
Ligands: LMU
Released: 10 Jul 2013

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

Secondary structure: helices and β-sheets

4ATV contains 80 α-helices and 8 β-strands across 4 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.

Chains A and C: 20 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	11-30	20
α-helix	35-42	8
β-strand	46-50	5	1
β-strand	53-57	5	1
α-helix	59-85	27
α-helix	95-113	19
α-helix	123-125	3
α-helix	134-141	8
α-helix	145-147	3
α-helix	150-174	25
α-helix	181-199	19
α-helix	205-219	15
α-helix	223-236	14
α-helix	241-243	3
α-helix	247-258	12
α-helix	259-263	5
α-helix	264-271	8
α-helix	287-297	11
α-helix	299-313	15
α-helix	327-334	8
α-helix	339-349	11
α-helix	357-378	22

Chains B and D: 20 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	11-30	20
α-helix	35-42	8
β-strand	45-50	6	1
β-strand	53-58	6	1
α-helix	59-85	27
α-helix	95-113	19
α-helix	123-127	5
α-helix	134-141	8
α-helix	145-147	3
α-helix	150-174	25
α-helix	181-199	19
α-helix	205-218	14
α-helix	223-235	13
α-helix	241-243	3
α-helix	247-258	12
α-helix	259-263	5
α-helix	264-271	8
α-helix	287-297	11
α-helix	299-313	15
α-helix	327-334	8
α-helix	339-349	11
α-helix	355-378	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Na(+)/h(+) antiporter nhaa	A, B, C, D	protein	401	ESCHERICHIA COLI	P13738 (AlphaFold model)

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

>4ATV_1 NA(+)/H(+) ANTIPORTER NHAA (chains A, B, C, D)
MKHLHRFFSSDASGGIILIIAAILAMIMANSGATSGWYHDFLETPVQLRVGSLEINKNML
LWINDALMAVFFLLVGLEVKRELMQGSLASLRQAAFPVIAAIGGMIVPTLLYLAFNYADP
ITREGWAIPAATDIAFALGVLALLGSRVPLALKIFLMALAIIDDLGAIIIIALFYTNDLS
MASLGVAAVAIAVLAVLNLCGARRTGVYILVGVVLWTAVLKSGVHATLAGVIVGFFIPLK
EKHGRSPAKRLEHVLHPWVAYLILPLFAFANAGVSLGGVTLDGLTSILPLGIIAGMLIGK
PLGISLFCWLALRLKLAHLPEGTTYQQIMVVGILCGIGFTMSIFIASLAFGSVDPELINW
AKLGILVGSISSAVIGYSWLRVRLRPSVEFRVPGSENLYFQ

Ligands and cofactors

ID	Name	Formula	Copies
LMU	Dodecyl-alpha-D-maltoside	C24 H46 O11	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Crystal structure of the sodium-proton antiporter NhaA dimer and new mechanistic insights. Lee, C., Yashiro, S., Dotson, D.L. et al. J Gen Physiol (2014) 144:529-544. DOI 10.1085/jgp.201411219 · PubMed

Other PDB entries of the same protein (UniProt P13738 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7S24 2.2 Å, Crystal structure of the Na+/H+ antiporter NhaA at pH 6.5
9RH1 2.7 Å, Cryo-EM structure of the consensus inward-facing apo NhaA dimer at pH 7.5
9RH2 2.7 Å, Cryo-EM structure of the inward-facing apo NhaA in the unplugged state at pH 7.5
9RH3 2.7 Å, Cryo-EM structure of the inward-facing apo NhaA in the plugged state at pH 7.5
9RHB 2.9 Å, Cryo-EM structure of the inward-facing apo NhaA in the open-funnel state at pH 8.5
9RHF 3.0 Å, Cryo-EM structure of the inward-facing sodium-bound NhaA at pH 8.5
9RH4 3.1 Å, Cryo-EM structure of the inward-facing apo NhaA with flexible N-terminus at pH 7.5
9RH8 3.1 Å, Cryo-EM structure of the inward-facing apo NhaA in the unplugged state at pH 5.5
9RH9 3.1 Å, Cryo-EM structure of the inward-facing apo NhaA in the plugged state at pH 5.5
9RHC 3.2 Å, Cryo-EM structure of the inward-facing apo NhaA in the unplugged state at pH 8.5
9RHD 3.2 Å, Cryo-EM structure of the inward-facing apo NhaA in the plugged state at pH 8.5
9RH5 3.3 Å, Cryo-EM structure of the inward-facing apo NhaA in the unplugged state at pH 6.3

Browse structure collections

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