2R9H: Q207C Mutant of CLC-ec1

Crystal Structure of Q207C Mutant of CLC-ec1 in complex with Fab. Determined by X-ray diffraction at 3.1 Å resolution. Released 20 Nov 2007.

Method: X-ray diffraction
Resolution: 3.1 Å
Organisms: Escherichia coli, Mus musculus
Chains: 6
Atoms: 13,221
Mol. weight: 188.37 kDa
Released: 20 Nov 2007

Explore 2R9H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2R9H contains 72 α-helices and 87 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, 2 β-strands

Element	Residues	Length	Sheet
α-helix	18-27	10
α-helix	33-70	38
α-helix	75-100	26
α-helix	102-104	3
α-helix	109-116	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	215-232	18
α-helix	249-251	3
α-helix	252-284	33
α-helix	288-308	21
α-helix	319-324	6
α-helix	330-348	19
β-strand	355	1	1
α-helix	357-378	22
α-helix	380-382	3
α-helix	386-394	9
α-helix	397-401	5
α-helix	405-416	12
α-helix	419-421	3
α-helix	422-437	16
α-helix	444-456	13

Chain B: 24 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	19-25	7
α-helix	33-70	38
α-helix	75-100	26
α-helix	102-104	3
α-helix	109-116	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	215-232	18
α-helix	249-251	3
α-helix	252-284	33
α-helix	288-308	21
α-helix	319-324	6
α-helix	330-348	19
β-strand	355	1	2
α-helix	357-378	22
α-helix	380-382	3
α-helix	386-394	9
α-helix	396-400	5
α-helix	405-416	12
α-helix	419-421	3
α-helix	422-438	17
α-helix	444-456	13

Chain C: 6 helices, 21 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	33-39	7	4
β-strand	45-51	7	4
β-strand	58-60	3	4
α-helix	65-67	3
β-strand	68-73	6	3
β-strand	78-84	7	3
α-helix	88-90	3
β-strand	92-100	9	4
β-strand	107-111	5	4
β-strand	115-119	5	4
α-helix	122-124	3
β-strand	125	1	5
β-strand	128-131	4	6
β-strand	143-153	11	6
β-strand	154	1	5
β-strand	159-162	4	7
α-helix	163-165	3
β-strand	171-173	3	6
α-helix	174-176	3
β-strand	177-179	3	6
β-strand	182-192	11	6
β-strand	202-207	6	7
α-helix	208-210	3
β-strand	212-217	6	7

Chain D: 5 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	8
β-strand	10-13	4	9
β-strand	19-25	7	8
β-strand	33-37	5	9
β-strand	43-48	6	9
β-strand	52-53	2	9
β-strand	61-66	6	8
β-strand	69-74	6	8
α-helix	79-81	3
β-strand	84-89	6	9
β-strand	96-97	2	9
β-strand	102-105	4	9
β-strand	110	1	10
β-strand	113-117	5	11
α-helix	118-120	3
α-helix	121-125	5
β-strand	128-138	11	11
β-strand	139	1	10
β-strand	144-149	6	12
β-strand	152-154	3	12
β-strand	158-162	5	11
α-helix	163-164	2
β-strand	172-181	10	11
α-helix	182-186	5
β-strand	190-196	7	12
β-strand	204-209	6	12

Chain E: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	13
β-strand	10-12	3	14
β-strand	18-25	8	13
β-strand	34-39	6	14
β-strand	45-51	7	14
β-strand	58-60	3	14
β-strand	68-73	6	13
β-strand	78-83	6	13
α-helix	88-90	3
β-strand	92-100	9	14
β-strand	107-111	5	14
β-strand	115-119	5	14
β-strand	125	1	15
β-strand	128-132	5	16
β-strand	143-153	11	16
β-strand	154	1	15
β-strand	159-162	4	17
α-helix	163-165	3
β-strand	171-173	3	16
α-helix	174-176	3
β-strand	177-179	3	16
β-strand	182-192	11	16
α-helix	193-195	3
β-strand	202-207	6	17
α-helix	208-210	3
β-strand	212-217	6	17
α-helix	219-221	3

Chain F: 7 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4-6	3	18
β-strand	10-13	4	19
β-strand	19-29	11	18
β-strand	33-37	5	19
β-strand	44-48	5	19
β-strand	52-53	2	19
α-helix	54	1
β-strand	61-74	14	18
α-helix	79-81	3
β-strand	84-89	6	19
β-strand	96-97	2	19
β-strand	101-105	5	19
β-strand	110	1	20
β-strand	113-117	5	21
α-helix	118-120	3
α-helix	121-124	4
β-strand	128-138	11	21
β-strand	139	1	20
β-strand	143-149	7	22
β-strand	152-154	3	22
β-strand	158-162	5	21
α-helix	163-166	4
β-strand	172-181	10	21
α-helix	182-186	5
β-strand	190-197	8	22
β-strand	200-209	10	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
H(+)/Cl(-) exchange transporter clcA	A, B	protein	444	Escherichia coli	P37019 (AlphaFold model)
Fab fragment	C, E	protein	221	Mus musculus	P01808 (AlphaFold model)
Fab fragment	D, F	protein	211	Mus musculus	P01837 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2R9H_1 H(+)/Cl(-) exchange transporter clcA (chains A, B)
RRRQLIRQLLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWLQNQRMGALVHTADNYP
LLLTVAFLCSAVLAMFGYFLVRKYAPEAGGSGIPEIEGALEDQRPVRWWRVLPVKFFGGL
GTLGGGMVLGREGPTVQIGGNIGRMVLDIFRLKGDEARHTLLATGAAAGLAAAFNAPLAG
ILFIIEEMRPCFRYTLISIKAVFIGVIMSTIMYRIFNHEVALIDVGKLSDAPLNTLWLYL
ILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGGLCGLLGFVAPATSGGG
FNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPMLALGTVLGTAFGMVAV
ELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQLILPMIITGLGATLLA
QFTGGKPLYSAILARTLAKQEAEQ

Sequence of entity 2 (C, E), FASTA

>2R9H_2 Fab fragment (chains C, E)
VRLLESGGGLVQPGGSLKLSCAASGFDYSRYWMSWVRQAPGKGLKWIGEINPVSSTINYT
PSLKDKFIISRDNAKDTLYLQISKVRSEDTALYYCARLYYGYGYWYFDVWGAGTTVTVSS
AKTTPPSVYPLAPGSAAAAASMVTLGCLVKGYFPEPVTVTWNSGSLAAGVHTFPAVLQAA
LYTLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRA

Sequence of entity 3 (D, F), FASTA

>2R9H_3 Fab fragment (chains D, F)
DIVLTQSPAIMSAAPGDKVTMTCSASSSVSYIHWYQQKSGTSPKRWIYDTSKLTSGVPVR
FSGSGSGTSYSLTINTMEAEDAATYYCQQWSSHPQTFGGGTKLEILRADAAPTVSIFPPS
SEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTL
TKDEYERHNSYTCEATHKTSTSPIVKSFNRA

Primary citation

Crystal Structure of Q207C Mutant of CLC-ec1 in complex with Fab. Miller, C., Nguitragool, W. To be published.

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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