2H2P: CLC-ec1

Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-. Determined by X-ray diffraction at 3.1 Å resolution. Released 30 May 2006.

Method: X-ray diffraction
Resolution: 3.1 Å
Organisms: Escherichia coli, Mus musculus
Chains: 6
Atoms: 13,231
Mol. weight: 193.72 kDa
Ligands: SEK
Released: 30 May 2006

Explore 2H2P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2H2P contains 64 α-helices and 95 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, 0 β-strands

Element	Residues	Length
α-helix	20-25	6
α-helix	35-69	35
α-helix	75-100	26
α-helix	109-116	8
α-helix	124-140	17
α-helix	148-165	18
α-helix	170-188	19
α-helix	193-199	7
α-helix	200-204	5
α-helix	215-233	19
α-helix	249-251	3
α-helix	253-284	32
α-helix	288-308	21
α-helix	319-325	7
α-helix	330-349	20
α-helix	357-378	22
α-helix	380-382	3
α-helix	387-393	7
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
α-helix	455-457	3

Chain B: 24 helices, 0 β-strands

Element	Residues	Length
α-helix	19-25	7
α-helix	35-70	36
α-helix	75-100	26
α-helix	109-116	8
α-helix	124-140	17
α-helix	148-162	15
α-helix	163-167	5
α-helix	171-188	18
α-helix	193-199	7
α-helix	200-204	5
α-helix	215-233	19
α-helix	249-251	3
α-helix	253-284	32
α-helix	288-308	21
α-helix	319-325	7
α-helix	330-349	20
α-helix	357-378	22
α-helix	380-382	3
α-helix	387-393	7
α-helix	397-400	4
α-helix	405-416	12
α-helix	419-421	3
α-helix	422-437	16
α-helix	444-455	12

Chain C: 4 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	11-12	2	2
β-strand	18-25	8	1
β-strand	33-39	7	3
β-strand	45-51	7	3
β-strand	58-60	3	3
β-strand	68-73	6	1
β-strand	78-83	6	1
β-strand	92-100	9	3
β-strand	107-108	2	3
β-strand	115-117	3	3
β-strand	118-119	2	2
α-helix	122-124	3
β-strand	125	1	4
β-strand	128-131	4	5
β-strand	143-145	3	6
β-strand	148-153	6	5
β-strand	154	1	4
β-strand	159-162	4	7
α-helix	163-165	3
β-strand	171-173	3	8
α-helix	174-176	3
β-strand	177-179	3	5
β-strand	182-186	5	5
β-strand	187-189	3	8
β-strand	190-192	3	6
α-helix	193-195	3
β-strand	202-207	6	7
β-strand	212-217	6	7

Chain D: 3 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	9
β-strand	10-13	4	10
β-strand	19-22	4	11
β-strand	23-24	2	9
β-strand	33-36	4	10
β-strand	44-45	2	10
β-strand	61-66	6	11
β-strand	69-74	6	11
β-strand	83-89	7	10
α-helix	95	1
β-strand	96-97	2	10
β-strand	101-105	5	10
β-strand	110	1	12
β-strand	113-116	4	13
α-helix	121-124	4
β-strand	128-138	11	13
β-strand	139	1	12
β-strand	144-146	3	14
β-strand	147-148	2	15
β-strand	153-154	2	15
β-strand	161-162	2	13
β-strand	172-181	10	13
α-helix	182-185	4
β-strand	190-191	2	16
β-strand	194-196	3	14
β-strand	208-209	2	16

Chain E: 5 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	17
β-strand	10-12	3	18
β-strand	17-25	9	17
α-helix	29-31	3
β-strand	34-39	6	19
β-strand	45-51	7	19
β-strand	60	1	19
β-strand	68-73	6	17
β-strand	78-84	7	17
α-helix	88-90	3
β-strand	93-98	6	19
β-strand	99-100	2	20
β-strand	107-108	2	20
β-strand	115-116	2	19
β-strand	117-119	3	18
β-strand	125	1	21
β-strand	128-132	5	22
α-helix	133-135	3
β-strand	143	1	23
β-strand	146-153	8	22
β-strand	154	1	21
β-strand	159-162	4	24
β-strand	167	1	24
β-strand	171-173	3	22
α-helix	174-176	3
β-strand	177-178	2	22
β-strand	183-189	7	22
β-strand	192	1	23
β-strand	202-207	6	24
α-helix	208-210	3
β-strand	212-217	6	24

Chain F: 4 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	25
β-strand	10-13	4	26
β-strand	19-29	11	25
β-strand	33-37	5	26
β-strand	44-48	5	26
β-strand	52-53	2	26
β-strand	61	1	25
β-strand	64-74	11	25
α-helix	79-81	3
β-strand	84-88	5	26
β-strand	97	1	26
β-strand	102-105	4	26
β-strand	110	1	27
β-strand	114-117	4	28
α-helix	118-120	3
α-helix	121-125	5
β-strand	129-138	10	28
β-strand	139	1	27
β-strand	144-149	6	29
β-strand	152-154	3	29
β-strand	158-162	5	28
β-strand	172-180	9	28
α-helix	182-187	6
β-strand	190-197	8	29
β-strand	200-209	10	29

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
CLC Cl transporter	A, B	protein	465	Escherichia coli	P37019 (AlphaFold model)
FAB fragment, heavy chain	C, E	protein	221	Mus musculus	P01808 (AlphaFold model)
FAB fragment, light chain	D, F	protein	211	Mus musculus	P01837 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2H2P_1 CLC Cl transporter (chains A, B)
MKTDTPSLETPQAARLRRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWL
QNQRMGALVHTADNYPLLLTVAFLCSAVLAMFGYFLVRKYAPEAGGSGIPEIEGALEDQR
PVRWWRVLPVKFFGGLGTLGGGMVLGREGPTVQIGGNIGRMVLDIFRLKGDEARHTLLAT
GAAAGLAAAFNAPLAGILFIIEEMRPQFRYTLISIKAVFIGVIMSTIMYRIFNHEVALID
VGKLSDAPLNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGG
LCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPM
LALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQ
LILPMIITGLGATLLAQFTGGKPLYSAILARTLAKQEAEQLARSK

Sequence of entity 2 (C, E), FASTA

>2H2P_2 FAB fragment, heavy chain (chains C, E)
VRLLESGGGLVQPGGSLKLSCAASGFDYSRYWMSWVRQAPGKGLKWIGEINPVSSTINYT
PSLKDKFIISRDNAKDTLYLQISKVRSEDTALYYCARLYYGYGYWYFDVWGAGTTVTVSS
AKTTPPSVYPLAPGSAAAAASMVTLGCLVKGYFPEPVTVTWNSGSLAAGVHTFPAVLQAA
LYTLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRA

Sequence of entity 3 (D, F), FASTA

>2H2P_3 FAB fragment, light chain (chains D, F)
DIVLTQSPAIMSAAPGDKVTMTCSASSSVSYIHWYQQKSGTSPKRWIYDTSKLTSGVPVR
FSGSGSGTSYSLTINTMEAEDAATYYCQQWSSHPQTFGGGTKLEILRADAAPTVSIFPPS
SEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL
TKDEYERHNSYTCEATHKTSTSPIVKSFNRA

Ligands and cofactors

ID	Name	Formula	Copies
SEK	Selenocyanate ion	C N Se	8

Primary citation

Uncoupling of a CLC Cl(-)/H(+) Exchange Transporter by Polyatomic Anions. Nguitragool, W., Miller, C. J Mol Biol (2006) 362:682-690. DOI 10.1016/j.jmb.2006.07.006 · 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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