2H2S: E148A mutant of CLC-ec1 in SeCN-

Crystal Structure of E148A mutant of CLC-ec1 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: 13,221
Mol. weight: 193.4 kDa
Ligands: SEK
Released: 30 May 2006

Explore 2H2S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2H2S contains 61 α-helices and 102 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	33-68	36
α-helix	75-100	26
α-helix	110-116	7
α-helix	124-138	15
β-strand	146	1	1
α-helix	148-165	18
α-helix	172-190	19
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	310-312	3
α-helix	319-324	6
α-helix	330-349	20
β-strand	355	1	1
α-helix	357-378	22
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	446-458	13

Chain B: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	20-25	6
α-helix	33-68	36
α-helix	75-100	26
α-helix	110-116	7
α-helix	124-138	15
β-strand	146	1	2
α-helix	148-165	18
α-helix	170-190	21
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	310-312	3
α-helix	319-324	6
α-helix	330-349	20
β-strand	355	1	2
α-helix	357-378	22
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	446-455	10

Chain C: 4 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	3
β-strand	11-12	2	4
β-strand	19-25	7	3
β-strand	33-39	7	5
β-strand	45-51	7	5
β-strand	58-60	3	5
α-helix	65-67	3
β-strand	68-73	6	3
β-strand	78-83	6	3
β-strand	92-100	9	5
β-strand	107-110	4	5
β-strand	115-117	3	5
β-strand	118-119	2	4
α-helix	123-124	2
β-strand	125	1	6
β-strand	128-131	4	7
β-strand	143-145	3	8
β-strand	148-153	6	7
β-strand	154	1	6
β-strand	162	1	9
α-helix	163-165	3
β-strand	171-173	3	7
α-helix	174-176	3
β-strand	177-178	2	7
β-strand	183-189	7	7
β-strand	190-192	3	8
β-strand	202-207	6	9
β-strand	212-217	6	9

Chain D: 6 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	10
β-strand	12-13	2	11
β-strand	19-25	7	10
β-strand	33-37	5	12
β-strand	44-46	3	12
β-strand	47	1	13
β-strand	48	1	12
β-strand	53	1	13
β-strand	61	1	10
β-strand	64-66	3	10
β-strand	69-74	6	10
β-strand	83-88	6	12
α-helix	95	1
β-strand	97	1	12
β-strand	101-103	3	12
β-strand	104-105	2	11
α-helix	106	1
α-helix	110-112	3
β-strand	113-116	4	14
α-helix	121-124	4
β-strand	128-136	9	14
β-strand	144	1	15
β-strand	147-149	3	16
β-strand	153	1	16
β-strand	158-162	5	14
α-helix	163-164	2
β-strand	173-181	9	14
α-helix	182-185	4
β-strand	190-193	4	16
β-strand	196	1	15
β-strand	206-209	4	16

Chain E: 2 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	17
β-strand	11-12	2	18
β-strand	18-25	8	17
β-strand	34-39	6	19
β-strand	45-51	7	19
β-strand	60	1	19
β-strand	68	1	17
β-strand	71-73	3	17
β-strand	78-83	6	17
α-helix	88-90	3
β-strand	92-100	9	19
β-strand	107-111	5	19
β-strand	116-117	2	19
β-strand	118-119	2	18
β-strand	125	1	20
β-strand	128-130	3	21
β-strand	143	1	22
β-strand	149-153	5	21
β-strand	154	1	20
β-strand	159-162	4	23
β-strand	172-173	2	24
α-helix	174-176	3
β-strand	177-179	3	21
β-strand	182-186	5	21
β-strand	187-188	2	24
β-strand	192	1	22
β-strand	202-207	6	23
β-strand	212-217	6	23

Chain F: 3 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	25
β-strand	10-13	4	26
β-strand	19-25	7	25
β-strand	33-37	5	26
β-strand	44-48	5	26
β-strand	52-53	2	26
β-strand	61-66	6	25
β-strand	69-74	6	25
α-helix	79-81	3
β-strand	84-89	6	26
β-strand	96-97	2	26
β-strand	102-105	4	26
β-strand	110	1	27
β-strand	116-117	2	28
α-helix	121-124	4
β-strand	129-138	10	28
β-strand	139	1	27
β-strand	144	1	29
β-strand	147-149	3	30
β-strand	152-154	3	30
β-strand	158-163	6	28
α-helix	164	1
β-strand	172-180	9	28
β-strand	190-195	6	30
β-strand	196	1	29
β-strand	204-209	6	30

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

>2H2S_1 CLC Cl transporter (chains A, B)
MKTDTPSLETPQAARLRRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWL
QNQRMGALVHTADNYPLLLTVAFLCSAVLAMFGYFLVRKYAPEAGGSGIPEIEGALEDQR
PVRWWRVLPVKFFGGLGTLGGGMVLGRAGPTVQIGGNIGRMVLDIFRLKGDEARHTLLAT
GAAAGLAAAFNAPLAGILFIIEEMRPQFRYTLISIKAVFIGVIMSTIMYRIFNHEVALID
VGKLSDAPLNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGG
LCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPM
LALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQ
LILPMIITGLGATLLAQFTGGKPLYSAILARTLAKQEAEQLARSK

Sequence of entity 2 (C, E), FASTA

>2H2S_2 FAB fragment, heavy chain (chains C, E)
VRLLESGGGLVQPGGSLKLSCAASGFDYSRYWMSWVRQAPGKGLKWIGEINPVSSTINYT
PSLKDKFIISRDNAKDTLYLQISKVRSEDTALYYCARLYYGYGYWYFDVWGAGTTVTVSS
AKTTPPSVYPLAPGSAAAAASMVTLGCLVKGYFPEPVTVTWNSGSLAAGVHTFPAVLQAA
LYTLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRA

Sequence of entity 3 (D, F), FASTA

>2H2S_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	6

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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