3TLW: Glr4197 protein

The GLIC pentameric Ligand-Gated Ion Channel Loop2-21' oxidized mutant in a locally-closed conformation (LC2 subtype). Determined by X-ray diffraction at 2.6 Å resolution. Released 16 May 2012.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Gloeobacter violaceus
Chains: 5
Atoms: 12,763
Mol. weight: 183.31 kDa
Ligands: LMT
Released: 16 May 2012

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

Secondary structure: helices and β-sheets

3TLW contains 68 α-helices and 65 β-strands across 5 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: 13 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	14-15	2
β-strand	16-31	16	1
β-strand	36-48	13	1
α-helix	50-52	3
β-strand	64-65	2	1
α-helix	68-70	3
β-strand	76-78	3	2
β-strand	81	1	1
β-strand	86-94	9	1
β-strand	99-111	13	1
β-strand	123-133	11	2
β-strand	140-144	5	1
α-helix	146-148	3
β-strand	150-151	2	1
β-strand	157	1	2
β-strand	160-176	17	2
β-strand	179-192	14	2
α-helix	197	1
α-helix	198-202	5
α-helix	203-212	10
α-helix	213-217	5
α-helix	221-242	22
α-helix	246-248	3
α-helix	254-281	28
α-helix	285-314	30

Chain B: 14 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	14-15	2
β-strand	16-31	16	3
β-strand	36-48	13	3
α-helix	50-52	3
α-helix	56-59	4
β-strand	64-65	2	3
α-helix	68-70	3
β-strand	76-78	3	4
β-strand	81	1	3
β-strand	86-94	9	3
β-strand	99-111	13	3
β-strand	123-133	11	4
β-strand	140-144	5	3
α-helix	146-148	3
β-strand	150-151	2	3
β-strand	157	1	4
β-strand	160-176	17	4
β-strand	179-192	14	4
α-helix	197	1
α-helix	198-202	5
α-helix	203-212	10
α-helix	213-217	5
α-helix	221-242	22
α-helix	246-248	3
α-helix	254-281	28
α-helix	285-314	30

Chain C: 14 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	14-15	2
β-strand	16-31	16	5
β-strand	36-48	13	5
α-helix	50-52	3
α-helix	56-59	4
β-strand	64-65	2	5
α-helix	68-70	3
β-strand	76-78	3	6
β-strand	81	1	5
β-strand	86-94	9	5
β-strand	99-111	13	5
β-strand	123-133	11	6
β-strand	140-144	5	5
α-helix	146-148	3
β-strand	150-151	2	5
β-strand	157	1	6
β-strand	160-176	17	6
β-strand	179-192	14	6
α-helix	197	1
α-helix	198-202	5
α-helix	203-212	10
α-helix	213-217	5
α-helix	221-241	21
α-helix	246-248	3
α-helix	254-281	28
α-helix	285-314	30

Chain D: 13 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	14-15	2
β-strand	16-31	16	7
β-strand	36-48	13	7
α-helix	50-52	3
α-helix	56-59	4
β-strand	64-65	2	7
α-helix	68-70	3
β-strand	76-78	3	8
β-strand	81	1	7
β-strand	86-94	9	7
β-strand	99-111	13	7
β-strand	123-133	11	8
β-strand	140-144	5	7
α-helix	146-148	3
β-strand	150-151	2	7
β-strand	157	1	8
β-strand	160-176	17	8
β-strand	179-192	14	8
α-helix	197	1
α-helix	198-202	5
α-helix	203-212	10
α-helix	213-217	5
α-helix	221-242	22
α-helix	254-281	28
α-helix	285-314	30

Chain E: 14 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	15	1
β-strand	16-31	16	9
β-strand	36-48	13	9
α-helix	50-52	3
α-helix	56-59	4
β-strand	64-65	2	9
α-helix	68-70	3
β-strand	76-78	3	10
β-strand	81	1	9
β-strand	86-94	9	9
β-strand	99-111	13	9
β-strand	123-133	11	10
β-strand	140-144	5	9
α-helix	146-148	3
β-strand	150-151	2	9
β-strand	157	1	10
β-strand	160-176	17	10
β-strand	179-192	14	10
α-helix	197	1
α-helix	198-202	5
α-helix	203-212	10
α-helix	213-217	5
α-helix	221-242	22
α-helix	246-248	3
α-helix	254-281	28
α-helix	285-314	30

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glr4197 protein	A, B, C, D, E	protein	321	Gloeobacter violaceus	Q7NDN8 (AlphaFold model)

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

>3TLW_1 Glr4197 protein (chains A, B, C, D, E)
GSAAAQDMVSPPPPIADEPLTVNTGIYLIESYSLDDCAETFKVNAFLSLSWKDRRLAFDP
VRSGVRVKTYEPEAIWIPEIRFVNVENARDADVVDISVSPDGTVQYLERFSARVLSPLDF
RRYPFDSQTLHIYLIVRSVDTRNIVLAVDLEKVGKNDDVFLTGWDIESFTAVVKPANFAL
EDRLESKLDYQLRISRQYFSYIPNIILPMLFILFISWTAFWSTSYEANVTLVVSTLIAHI
AFNILVETCLPKTPYMTYTGAIIFMIYLFYFVAVIEVTVQHYLKVESQPARAASITRASR
IAFPVVFLLANIILAFLFFGF

Ligands and cofactors

ID	Name	Formula	Copies
LMT	Dodecyl-beta-D-maltoside	C24 H46 O11	1

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

Primary citation

A locally closed conformation of a bacterial pentameric proton-gated ion channel. Prevost, M.S., Sauguet, L., Nury, H. et al. Nat Struct Mol Biol (2012) 19:642-649. DOI 10.1038/nsmb.2307 · PubMed

Other PDB entries of the same protein (UniProt Q7NDN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9LBD 2.14 Å, Cryo-EM structure of nanodisc (PE:PS:PC) reconstituted GLIC F116A mutant at pH 2.5
6HZW 2.22 Å, THE GLIC PENTAMERIC LIGAND-GATED ION CHANNEL 2.22 resolution
3IGQ 2.3 Å, Crystal structure of the extracellular domain of a bacterial pentameric ligand-gated ion…
6F0U 2.35 Å, GLIC mutant E35A
4HFI 2.4 Å, The GLIC pentameric Ligand-Gated Ion Channel at 2.4 A resolution
6F0R 2.5 Å, GLIC mutant E82Q
6F0Z 2.5 Å, GLIC mutant D88N
6HJZ 2.5 Å, Xray structure of GLIC in complex with succinate
6HZ1 2.5 Å, The glic pentameric ligand-gated ion channel mutant E243C
6HY5 2.58 Å, The glic pentameric ligand-gated ion channel mutant Q193C
5IUX 2.6 Å, GLIC-V135C bimane labelled X-ray structure
6F16 2.6 Å, GLIC mutant H277Q

Browse structure collections

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