2EXW: EcClC-Fab complex in the absence of bound ions

Crystal structure of a EcClC-Fab complex in the absence of bound ions. Determined by X-ray diffraction at 3.2 Å resolution. Released 24 Jan 2006.

Method: X-ray diffraction
Resolution: 3.2 Å
Organisms: Escherichia coli, Mus musculus
Chains: 6
Atoms: 13,223
Mol. weight: 194.6 kDa
Released: 24 Jan 2006

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

Secondary structure: helices and β-sheets

2EXW contains 59 α-helices and 101 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: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-25	8
α-helix	33-65	33
α-helix	75-100	26
α-helix	110-117	8
α-helix	124-140	17
β-strand	146	1	1
α-helix	148-165	18
α-helix	171-190	20
α-helix	193-199	7
α-helix	200-204	5
α-helix	215-233	19
α-helix	249-251	3
α-helix	253-282	30
α-helix	288-308	21
α-helix	319-325	7
α-helix	330-348	19
β-strand	355	1	1
α-helix	358-378	21
α-helix	380-382	3
α-helix	386-392	7
α-helix	396-400	5
α-helix	405-416	12
α-helix	419-421	3
α-helix	422-437	16
α-helix	444-454	11

Chain B: 22 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	21-25	5
α-helix	33-68	36
α-helix	76-100	25
α-helix	110-117	8
α-helix	124-140	17
β-strand	146	1	2
α-helix	148-165	18
α-helix	171-190	20
α-helix	193-199	7
α-helix	200-204	5
α-helix	215-233	19
α-helix	249-251	3
α-helix	253-282	30
α-helix	288-308	21
α-helix	319-324	6
α-helix	330-348	19
β-strand	355	1	2
α-helix	358-378	21
α-helix	386-393	8
α-helix	397-400	4
α-helix	405-416	12
α-helix	419-421	3
α-helix	422-437	16
α-helix	444-454	11

Chain C: 3 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	3
β-strand	10-12	3	4
β-strand	17-25	9	3
β-strand	33	1	5
β-strand	34-39	6	4
β-strand	45-51	7	4
β-strand	58-60	3	4
β-strand	68-73	6	3
β-strand	78-84	7	3
α-helix	88-90	3
β-strand	92-96	5	4
β-strand	99-100	2	5
β-strand	107-108	2	5
β-strand	115-119	5	4
α-helix	123-124	2
β-strand	125	1	6
α-helix	126-127	2
β-strand	128-131	4	7
β-strand	143-146	4	8
β-strand	148-153	6	7
β-strand	154	1	6
β-strand	159-162	4	9
β-strand	171-172	2	8
β-strand	177-179	3	7
β-strand	182-186	5	7
β-strand	188-192	5	8
β-strand	202-207	6	9
β-strand	212-217	6	9

Chain D: 4 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	10
β-strand	10-13	4	11
β-strand	18-24	7	10
β-strand	33-36	4	11
β-strand	44-45	2	11
β-strand	47-48	2	12
β-strand	52-53	2	12
α-helix	54	1
β-strand	61-66	6	10
β-strand	69-75	7	10
β-strand	83-89	7	11
β-strand	96-97	2	11
β-strand	101-105	5	11
β-strand	113-114	2	13
β-strand	117	1	14
α-helix	118-120	3
α-helix	121-124	4
β-strand	128-132	5	14
β-strand	135-136	2	13
β-strand	144-149	6	15
β-strand	153-154	2	15
β-strand	160-162	3	13
β-strand	173-176	4	13
β-strand	177-181	5	14
α-helix	182-186	5
β-strand	190	1	16
β-strand	191-196	6	15
β-strand	204	1	15
β-strand	209	1	16

Chain E: 3 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	17
β-strand	10-12	3	18
β-strand	18-25	8	17
β-strand	33-39	7	18
β-strand	45-46	2	18
β-strand	49	1	19
β-strand	50	1	18
β-strand	60	1	19
β-strand	70-73	4	17
α-helix	74-76	3
β-strand	78-83	6	17
α-helix	88-90	3
β-strand	92-100	9	18
β-strand	107-111	5	18
β-strand	116-119	4	18
β-strand	125	1	20
β-strand	128-132	5	21
β-strand	143-153	11	21
β-strand	154	1	20
β-strand	159-162	4	22
β-strand	167	1	22
β-strand	171-173	3	21
α-helix	174-176	3
β-strand	177-178	2	21
β-strand	183-192	10	21
β-strand	202-207	6	22
β-strand	212-217	6	22

Chain F: 4 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	23
β-strand	10-13	4	24
β-strand	18-25	8	23
β-strand	33	1	25
β-strand	34-37	4	24
β-strand	44-48	5	24
β-strand	52-53	2	24
β-strand	61-66	6	23
β-strand	69-75	7	23
α-helix	79-81	3
β-strand	84-85	2	24
β-strand	88-89	2	25
α-helix	95	1
β-strand	96-97	2	25
β-strand	102-105	4	24
β-strand	114-116	3	26
α-helix	121-124	4
β-strand	128-135	8	26
β-strand	138	1	27
β-strand	145-149	5	28
β-strand	152	1	28
β-strand	158-162	5	26
β-strand	172	1	27
β-strand	174-181	8	26
α-helix	182-186	5
β-strand	190-195	6	28
β-strand	204-209	6	28

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

>2EXW_1 H(+)/Cl(-) exchange transporter clcA (chains A, B)
MKTDTPSLETPQAARLRRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWL
QNQRMGALVHTADNYPLLLTVAFLCSAVLAMFGYFLVRKYAPEAGGSGIPEIEGALEDQR
PVRWWRVLPVKFFGGLGTLGGGMVLGREGPTVQIGGNIGRMVLDIFRLKGDEARHTLLAT
GAAAGLAAAFNAPLAGILFIIEEMRPQFRYTLISIKAVFIGVIMSTIMYRIFNHEVALID
VGKLSDAPLNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGG
LCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPM
LALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQ
LILPMIITGLGATLLAQFTGGKPLYSAILARTLAKQEAEQLARSKAASASENT

Sequence of entity 2 (C, E), FASTA

>2EXW_2 Fab Fragment (Heavy Chain) (chains C, E)
EVRLLESGGGLVQPGGSLKLSCAASGFDYSRYWMSWVRQAPGKGLKWIGEINPVSSTINY
TPSLKDKFIISRDNAKDTLYLQISKVRSEDTALYYCARLYYGYGYWYFDVWGAGTTVTVS
SAKTTPPSVYPLAPGSAAAAASMVTLGCLVKGYFPEPVTVTWNSGSLAAGVHTFPAVLQA
ALYTLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRA

Sequence of entity 3 (D, F), FASTA

>2EXW_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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