3RHW: C. elegans glutamate-gated chloride channel

C. elegans glutamate-gated chloride channel (GluCl) in complex with Fab and ivermectin. Determined by X-ray diffraction at 3.26 Å resolution. Released 25 May 2011.

Method: X-ray diffraction
Resolution: 3.26 Å
Organisms: Caenorhabditis elegans, Mus musculus
Chains: 15
Atoms: 29,197
Mol. weight: 437.99 kDa
Ligands: LMT, NAG, OCT, UND
Released: 25 May 2011

Explore 3RHW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3RHW contains 129 α-helices and 283 β-strands across 15 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: 14 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	2-11	10
α-helix	19-21	3
α-helix	27	1
β-strand	28-43	16	1
β-strand	48-60	13	1
α-helix	62-64	3
β-strand	76-78	3	1
α-helix	79-80	2
β-strand	90-91	2	2
β-strand	95-100	6	1
β-strand	108-113	6	1
β-strand	117-129	13	1
α-helix	137-139	3
β-strand	141-150	10	2
β-strand	158-162	5	1
β-strand	168-170	3	1
α-helix	175-177	3
β-strand	181-190	10	2
β-strand	193-194	2	3
β-strand	199-200	2	3
β-strand	202-211	10	2
α-helix	212	1
α-helix	214-216	3
α-helix	217-221	5
α-helix	222-232	11
α-helix	242-265	24
α-helix	275-302	28
α-helix	306-338	33

Chain B: 14 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	2-11	10
α-helix	19-21	3
α-helix	27	1
β-strand	28-43	16	4
β-strand	48-60	13	4
α-helix	62-64	3
β-strand	76-78	3	4
α-helix	79-80	2
β-strand	90-91	2	5
β-strand	95-100	6	4
β-strand	108-113	6	4
β-strand	117-129	13	4
α-helix	137-139	3
β-strand	141-150	10	5
β-strand	158-162	5	4
β-strand	168-170	3	4
α-helix	175-177	3
β-strand	181-190	10	5
β-strand	193-195	3	6
β-strand	198-200	3	6
β-strand	202-211	10	5
α-helix	212	1
α-helix	214-216	3
α-helix	217-221	5
α-helix	222-230	9
α-helix	242-265	24
α-helix	275-302	28
α-helix	306-338	33

Chains C, D and E: 14 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	2-11	10
α-helix	19-21	3
α-helix	27	1
β-strand	28-43	16	7
β-strand	48-60	13	7
α-helix	62-64	3
β-strand	76-78	3	7
α-helix	79-80	2
β-strand	90-91	2	8
β-strand	95-100	6	7
β-strand	108-113	6	7
β-strand	117-129	13	7
α-helix	137-139	3
β-strand	141-150	10	8
β-strand	158-162	5	7
β-strand	168-170	3	7
α-helix	175-177	3
β-strand	181-190	10	8
β-strand	193-194	2	9
β-strand	199-200	2	9
β-strand	202-211	10	8
α-helix	212	1
α-helix	214-216	3
α-helix	217-221	5
α-helix	222-230	9
α-helix	242-265	24
α-helix	275-302	28
α-helix	306-338	33

Chain F: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	16
β-strand	10-12	3	17
β-strand	18-25	8	16
α-helix	29-31	3
β-strand	34-39	6	17
β-strand	45-51	7	17
β-strand	58-60	3	17
α-helix	62-64	3
β-strand	65	1	16
β-strand	68-73	6	16
α-helix	74-76	3
β-strand	78-83	6	16
α-helix	88-90	3
β-strand	92-99	8	17
β-strand	109-112	4	17
β-strand	116-120	5	17
β-strand	126	1	18
β-strand	129-131	3	19
β-strand	150-154	5	19
β-strand	155	1	18
β-strand	160-163	4	20
α-helix	164-166	3
α-helix	175-177	3
β-strand	180	1	21
β-strand	183	1	21
β-strand	184-186	3	19
β-strand	204-208	5	20
β-strand	213-216	4	20

Chain G: 5 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	22
β-strand	10-12	3	23
β-strand	18-25	8	22
α-helix	29-31	3
β-strand	34-39	6	23
β-strand	45-51	7	23
β-strand	58-60	3	23
α-helix	62-64	3
β-strand	65	1	22
β-strand	68-73	6	22
α-helix	74-76	3
β-strand	78-83	6	22
α-helix	88-90	3
β-strand	92-99	8	23
β-strand	109-112	4	23
β-strand	116-120	5	23
β-strand	126	1	24
β-strand	129-132	4	25
β-strand	149-154	6	25
β-strand	155	1	24
β-strand	161-163	3	26
α-helix	164-166	3
β-strand	173-174	2	25
β-strand	178-179	2	25
β-strand	184-189	6	25
β-strand	203-206	4	26
β-strand	208	1	27
β-strand	213	1	27
β-strand	216-218	3	26

Chain H: 11 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	28
β-strand	10-12	3	29
β-strand	18-25	8	28
α-helix	29-31	3
β-strand	34-39	6	29
β-strand	45-51	7	29
β-strand	58-60	3	29
α-helix	62-64	3
β-strand	65	1	28
β-strand	68-73	6	28
α-helix	74-76	3
β-strand	78-83	6	28
α-helix	88-90	3
β-strand	92-99	8	29
β-strand	109-112	4	29
β-strand	116-120	5	29
α-helix	123-125	3
β-strand	126	1	30
β-strand	129-133	5	31
α-helix	134-136	3
α-helix	139-141	3
β-strand	144-154	11	31
β-strand	155	1	30
β-strand	160-163	4	32
α-helix	164-166	3
β-strand	172-174	3	31
α-helix	175-177	3
β-strand	178-180	3	31
β-strand	183-193	11	31
α-helix	194-196	3
β-strand	203-208	6	32
α-helix	209-211	3
β-strand	213-218	6	32

Chain I: 6 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	33
β-strand	10-12	3	34
β-strand	18-25	8	33
α-helix	29-31	3
β-strand	34-39	6	34
β-strand	45-51	7	34
β-strand	58-60	3	34
α-helix	62-64	3
β-strand	65	1	33
β-strand	68-73	6	33
α-helix	74-76	3
β-strand	78-83	6	33
α-helix	88-90	3
β-strand	92-99	8	34
β-strand	109-112	4	34
β-strand	116-120	5	34
β-strand	129-133	5	35
β-strand	144-152	9	35
β-strand	173-174	2	35
α-helix	175-176	2
β-strand	178-180	3	35
β-strand	183-193	11	35
α-helix	194-196	3
β-strand	203-206	4	36
β-strand	215-218	4	36

Chain J: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	37
β-strand	10-12	3	38
β-strand	18-25	8	37
α-helix	29-31	3
β-strand	34-39	6	38
β-strand	45-51	7	38
β-strand	58-60	3	38
α-helix	62-64	3
β-strand	65	1	37
β-strand	68-73	6	37
α-helix	74-76	3
β-strand	78-83	6	37
α-helix	88-90	3
β-strand	92-99	8	38
β-strand	109-112	4	38
β-strand	116-120	5	38
α-helix	123-125	3
β-strand	126	1	39
β-strand	129-133	5	40
β-strand	145-154	10	40
β-strand	155	1	39
β-strand	160-163	4	41
β-strand	172-174	3	40
α-helix	175-177	3
β-strand	178-180	3	40
β-strand	183-192	10	40
β-strand	203-208	6	41
β-strand	213-218	6	41

5 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Avermectin-sensitive glutamate-gated chloride channel GluCl alpha	A, B, C, D, E	protein	347	Caenorhabditis elegans	O17793
Mouse monoclonal Fab fragment, heavy chain	F, G, H, I, J	protein	221	Mus musculus	P01868 (AlphaFold model)
Mouse monoclonal Fab fragment, light chain	K, L, M, N, O	protein	210	Mus musculus	G0YP42 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>3RHW_1 Avermectin-sensitive glutamate-gated chloride channel GluCl alpha (chains A, B, C, D, E)
SDSKILAHLFTSGYDFRVRPPTDNGGPVVVSVNMLLRTISKIDVVNMEYSAQLTLRESWI
DKRLSYGVKGDGQPDFVILTVGHQIWMPDTFFPNEKQAYKHTIDKPNVLIRIHNDGTVLY
SVRISLVLSCPMYLQYYPMDVQQCSIDLASYAYTTKDIEYLWKEHSPLQLKVGLSSSLPS
FQLTNTSTTYCTSVTNTGIYSCLRTTIQLKREFSFYLLQLYIPSCMLVIVSWVSFWFDRT
AIPARVTLGVTTLLTMTAQSAGINSQLPPVSYIKAIDVWIGACMTFIFCALLEFALVNHI
ANAGTTEWNDISKRVDLISRALFPVLFFVFNILYWSRFGHHHHHHHH

Sequence of entity 2 (F, G, H, I, J), FASTA

>3RHW_2 Mouse monoclonal Fab fragment, heavy chain (chains F, G, H, I, J)
EVQLQQSGPELVRPGASMKISCKASGYSFTGYTMNWVKQSHGKNLEWIGLINPYNGGTSY
NQKFKGKATLTVDKSSSTAYMELLSLTSEDSAVYYCARDGDYYRYGRYFDYWGQGTTLTV
SSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQ
SDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVP

Sequence of entity 3 (K, L, M, N, O), FASTA

>3RHW_3 Mouse monoclonal Fab fragment, light chain (chains K, L, M, N, O)
QAVVTQESALTTSPGETVTLTCRSSTGAVTTINFANWVQEKPDHLFTGLIGGINNRAPGV
PARFSGSLIGDKAALTITGAQTEDEAIYFCALWYSNHWVFGGGTKLTVLGQPKSSPSVTL
FPPSSEELETNKATLVCTITDFYPGVVTVDWKVDGTPVTQGMETTQPSKQSNNKYMASSY
LTLTARAWERHSSYSCQVTHEGHTVEKSLS

Ligands and cofactors

ID	Name	Formula	Copies
LMT	Dodecyl-beta-D-maltoside	C24 H46 O11	3
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3
OCT	N-octane	C8 H18	3
UND	Undecane	C11 H24	1
IVM	(2aE,4E,5'S,6S,6'R,7S,8E,11R,13R,15S,17aR,20R,20aR,20bS)-6'-[(2S)-butan-2-yl]-2…	C48 H74 O14	5

Water and common crystallization additives (CL) are not listed.

Primary citation

Principles of activation and permeation in an anion-selective Cys-loop receptor. Hibbs, R.E., Gouaux, E. Nature (2011) 474:54-60. DOI 10.1038/nature10139 · PubMed

Other PDB entries of the same protein (UniProt O17793), best resolution first:

3RIF 3.35 Å, C. elegans glutamate-gated chloride channel (GluCl) in complex with Fab, ivermectin and…
3RI5 3.4 Å, C. elegans glutamate-gated chloride channel (GluCl) in complex with Fab, ivermectin and…
3RIA 3.8 Å, C. elegans glutamate-gated chloride channel (GluCl) in complex with Fab, ivermectin and…

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