2EZ0: S107A/E148Q/Y445A mutant of EcClC

Crystal structure of the S107A/E148Q/Y445A mutant of EcClC, in complex with a FaB fragment. Determined by X-ray diffraction at 3.54 Å resolution. Released 24 Jan 2006.

Method: X-ray diffraction
Resolution: 3.54 Å
Organisms: Escherichia coli, Mus musculus
Chains: 6
Atoms: 13,209
Mol. weight: 194.55 kDa
Released: 24 Jan 2006

Explore 2EZ0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2EZ0 contains 67 α-helices and 90 β-strands across 6 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: 24 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	18-25	8
α-helix	33-63	31
α-helix	75-98	24
β-strand	106	1	1
α-helix	109-115	7
α-helix	124-141	18
β-strand	146	1	2
α-helix	149-165	17
α-helix	171-190	20
α-helix	193-199	7
α-helix	200-204	5
α-helix	215-231	17
α-helix	249-251	3
α-helix	253-282	30
α-helix	288-305	18
α-helix	317-319	3
α-helix	320-325	6
α-helix	330-348	19
β-strand	353	1	1
β-strand	355	1	2
α-helix	358-378	21
α-helix	386-392	7
α-helix	393-395	3
α-helix	397-399	3
α-helix	405-414	10
α-helix	419-421	3
α-helix	422-437	16
α-helix	444-454	11

Chain B: 23 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	19-25	7
α-helix	33-63	31
α-helix	75-98	24
β-strand	106	1	3
α-helix	109-115	7
α-helix	124-141	18
β-strand	146	1	4
α-helix	149-165	17
α-helix	171-189	19
α-helix	193-200	8
α-helix	215-231	17
α-helix	243-245	3
α-helix	249-251	3
α-helix	253-282	30
α-helix	288-305	18
α-helix	317-319	3
α-helix	320-325	6
α-helix	330-348	19
β-strand	353	1	3
β-strand	355	1	4
α-helix	357-378	22
α-helix	387-392	6
α-helix	397-399	3
α-helix	405-416	12
α-helix	419-421	3
α-helix	424-437	14
α-helix	444-454	11

Chain C: 4 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	5
β-strand	10-12	3	6
β-strand	17-25	9	5
β-strand	33-39	7	6
β-strand	45-51	7	6
β-strand	58-60	3	6
β-strand	68-73	6	5
β-strand	78-84	7	5
α-helix	88-90	3
β-strand	92-100	9	6
β-strand	107-110	4	6
β-strand	115-119	5	6
β-strand	125	1	7
β-strand	128-131	4	8
β-strand	143-153	11	8
β-strand	154	1	7
β-strand	159-162	4	9
α-helix	163-165	3
β-strand	171-173	3	8
α-helix	174-176	3
β-strand	177-178	2	8
β-strand	183-192	10	8
α-helix	193-195	3
β-strand	202-207	6	9
β-strand	212-217	6	9

Chain D: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	10
β-strand	10-13	4	11
β-strand	19-24	6	10
β-strand	33-37	5	11
β-strand	44-48	5	11
β-strand	52-53	2	11
β-strand	61-66	6	10
β-strand	69-74	6	10
α-helix	79-81	3
β-strand	83-89	7	11
α-helix	95	1
β-strand	96-97	2	11
β-strand	101-105	5	11
β-strand	110	1	12
α-helix	111-112	2
β-strand	113-116	4	13
α-helix	118-120	3
α-helix	121-124	4
β-strand	128-138	11	13
β-strand	139	1	12
β-strand	143-149	7	14
β-strand	158-162	5	13
α-helix	163-164	2
β-strand	172-181	10	13
α-helix	182-186	5
β-strand	190-197	8	14
β-strand	204-205	2	14
β-strand	208-209	2	14

Chain E: 4 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	15
β-strand	10-12	3	16
β-strand	18-25	8	15
β-strand	33-39	7	16
β-strand	45-51	7	16
β-strand	58-60	3	16
β-strand	68-73	6	15
β-strand	78-83	6	15
α-helix	88-90	3
β-strand	92-100	9	16
β-strand	107-111	5	16
β-strand	116-119	4	16
β-strand	125	1	17
β-strand	128-131	4	18
β-strand	143-153	11	18
β-strand	154	1	17
β-strand	159-162	4	19
α-helix	163-165	3
β-strand	171-173	3	18
α-helix	174-176	3
β-strand	177-178	2	18
β-strand	183-192	10	18
α-helix	193-195	3
β-strand	202-207	6	19
β-strand	212-217	6	19

Chain F: 5 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	20
β-strand	10-13	4	21
β-strand	19-25	7	20
β-strand	33-37	5	21
β-strand	44-48	5	21
β-strand	52-53	2	21
β-strand	61-66	6	20
β-strand	69-74	6	20
α-helix	79-81	3
β-strand	84-89	6	21
α-helix	95	1
β-strand	96-97	2	21
β-strand	101-105	5	21
β-strand	114-117	4	22
α-helix	121-124	4
β-strand	128-138	11	22
β-strand	143-149	7	23
β-strand	158-162	5	22
α-helix	163-164	2
β-strand	172-181	10	22
α-helix	182-186	5
β-strand	190-197	8	23
β-strand	204-205	2	23
β-strand	208-209	2	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
H(+)/Cl(-) exchange transporter clcA	A, B	protein	473	Escherichia coli	P37019 (AlphaFold model)
Fab Fragment (Heavy Chain)	C, E	protein	222	Mus musculus	P01808 (AlphaFold model)
Fab Fragment (Light Chain)	D, F	protein	211	Mus musculus

Sequence of entity 1 (A, B), FASTA

>2EZ0_1 H(+)/Cl(-) exchange transporter clcA (chains A, B)
MKTDTPSLETPQAARLRRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWL
QNQRMGALVHTADNYPLLLTVAFLCSAVLAMFGYFLVRKYAPEAGGAGIPEIEGALEDQR
PVRWWRVLPVKFFGGLGTLGGGMVLGRQGPTVQIGGNIGRMVLDIFRLKGDEARHTLLAT
GAAAGLAAAFNAPLAGILFIIEEMRPQFRYTLISIKAVFIGVIMSTIMYRIFNHEVALID
VGKLSDAPLNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGG
LCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPM
LALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQ
LILPMIITGLGATLLAQFTGGKPLASAILARTLAKQEAEQLARSKAASASENT

Sequence of entity 2 (C, E), FASTA

>2EZ0_2 Fab Fragment (Heavy Chain) (chains C, E)
EVRLLESGGGLVQPGGSLKLSCAASGFDYSRYWMSWVRQAPGKGLKWIGEINPVSSTINY
TPSLKDKFIISRDNAKDTLYLQISKVRSEDTALYYCARLYYGYGYWYFDVWGAGTTVTVS
SAKTTPPSVYPLAPGSAAAAASMVTLGCLVKGYFPEPVTVTWNSGSLAAGVHTFPAVLQA
ALYTLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRA

Sequence of entity 3 (D, F), FASTA

>2EZ0_3 Fab Fragment (Light Chain) (chains D, F)
DIVLTQSPAIMSAAPGDKVTMTCSASSSVSYIHWYQQKSGTSPKRWIYDTSKLTSGVPVR
FSGSGSGTSYSLTINTMEAEDAATYYCQQWSSHPQTFGGGTKLEILRADAAPTVSIFPPS
SEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL
TKDEYERHNSYTCEATHKTSTSPIVKSFNRA

Primary citation

Ion-binding properties of the ClC chloride selectivity filter. Lobet, S., Dutzler, R. EMBO J (2006) 25:24-33. DOI 10.1038/sj.emboj.7600909 · 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
6V2J 2.62 Å, Crystal structure of ClC-ec1 triple mutant (E113Q, E148Q, E203Q)
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

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