6V2J: ClC-ec1 triple mutant

Crystal structure of ClC-ec1 triple mutant (E113Q, E148Q, E203Q). Determined by X-ray diffraction at 2.62 Å resolution. Released 20 May 2020.

Method: X-ray diffraction
Resolution: 2.62 Å
Organism: Escherichia coli (strain K12)
Chains: 1
Atoms: 3,310
Mol. weight: 52.22 kDa
Released: 20 May 2020

Explore 6V2J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6V2J contains 24 α-helices and 4 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: 24 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	31-67	37
α-helix	75-99	25
α-helix	102-104	3
β-strand	106	1	1
α-helix	109-116	8
α-helix	124-140	17
β-strand	146	1	2
α-helix	148-166	19
α-helix	171-190	20
α-helix	193-198	6
α-helix	199-203	5
α-helix	212-232	21
α-helix	244-246	3
α-helix	249-251	3
α-helix	253-284	32
α-helix	288-308	21
α-helix	310-312	3
α-helix	317-319	3
α-helix	320-324	5
α-helix	330-349	20
β-strand	353	1	1
β-strand	355	1	2
α-helix	357-378	22
α-helix	386-401	16
α-helix	405-416	12
α-helix	419-421	3
α-helix	422-438	17
α-helix	444-458	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
H(+)/Cl(-) exchange transporter ClcA	A	protein	489	Escherichia coli (strain K12)	P37019 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6V2J_1 H(+)/Cl(-) exchange transporter ClcA (chains A)
MKTDTPSLETPQAARLRRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWL
QNQRMGALVHTADNYPLLLTVAFLCSAVLAMFGYFLVRKYAPEAGGSGIPEIQGALEDQR
PVRWWRVLPVKFFGGLGTLGGGMVLGRQGPTVQIGGNIGRMVLDIFRLKGDEARHTLLAT
GAAAGLAAAFNAPLAGILFIIEQMRPQFRYTLISIKAVFIGVIMSTIMYRIFNHEVALID
VGKLSDAPLNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGG
LCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPM
LALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQ
LILPMIITGLGATLLAQFTGGKPLYSAILARTLAKQEAEQLARSKAASKGSGTLVPRGSG
GLEHHHHHH

Primary citation

A CLC-ec1 mutant reveals global conformational change and suggests a unifying mechanism for the CLC Cl - /H + transport cycle. Chavan, T.S., Cheng, R.C., Jiang, T. et al. Elife (2020) 9. DOI 10.7554/eLife.53479 · PubMed

Other PDB entries of the same protein (UniProt P37019 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4ENE 2.4 Å, Structure of the N- and C-terminal trimmed ClC-ec1 Cl-/H+ antiporter and Fab Complex
1OTS 2.51 Å, Structure of the Escherichia coli ClC Chloride channel and Fab Complex
8GA1 2.6 Å, CLC-ec1 R230C/L249C/C85A at pH 4.5 100mM Cl Swap
8GA5 2.6 Å, CLC-ec1 L25C/A450C/C85A at pH 4.5 100mM Cl Intermediate
6ADB 2.69 Å, Crystal structure of the E148N mutant CLC-ec1 in 20mM bromide
3DET 2.8 Å, Structure of the E148A, Y445A doubly ungated mutant of E.coli CLC_Ec1, Cl-/H+ antiporter
4KKL 2.85 Å, Structure of the E148A mutant of CLC-ec1 delta NC construct in 100mM fluoride
4KK8 2.86 Å, Structure of the E148Q mutant of CLC-ec1 deltaNC construct in 100mM fluoride
4KJQ 2.88 Å, Structure of the CLC-ec1 deltaNC construct in 100mM fluoride
3EJZ 2.9 Å, Structure of E203V mutant E.coli Cl-/H+ exchanger, CLC-ec1
7CVT 2.9 Å, Crystal structure of the C85A/L194A/H234C mutant CLC-ec1 with Fab fragment
8GAH 2.9 Å, CLC-ec1 L25C/A450C/C85A at pH 4.5 100mM Cl Twist

Browse structure collections

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