6L6I: HASIC1a co-crystallized with Mamb-1

hASIC1a co-crystallized with Mamb-1. Determined by X-ray diffraction at 3.24 Å resolution. Released 4 Nov 2020.

Method: X-ray diffraction
Resolution: 3.24 Å
Organism: Homo sapiens
Chains: 3
Atoms: 10,321
Mol. weight: 155.77 kDa
Ligands: NAG
Released: 4 Nov 2020

Explore 6L6I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6L6I contains 69 α-helices and 60 β-strands across 3 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, 20 β-strands

Element	Residues	Length	Sheet
α-helix	38-40	3
α-helix	43-69	27
β-strand	73-81	9	1
β-strand	85-86	2	2
β-strand	89-94	6	3
α-helix	105-111	7
α-helix	132-141	10
α-helix	149-151	3
α-helix	154-161	8
α-helix	163-164	2
α-helix	165-168	4
β-strand	169-174	6	1
β-strand	177-178	2	1
α-helix	181-183	3
β-strand	184-189	6	3
β-strand	192-197	6	3
α-helix	204-207	4
β-strand	208-209	2	2
β-strand	217-223	7	1
α-helix	226-228	3
α-helix	230-231	2
β-strand	243	1	4
β-strand	245-250	6	3
α-helix	258-261	4
β-strand	263-265	3	3
β-strand	269-281	13	1
β-strand	291	1	5
α-helix	307-323	17
β-strand	326	1	6
α-helix	335	1
β-strand	336	1	6
α-helix	337-338	2
α-helix	339-341	3
α-helix	342-346	5
α-helix	347-355	9
α-helix	358-360	3
α-helix	364-365	2
β-strand	366	1	5
β-strand	368-380	13	1
α-helix	384-394	11
α-helix	398-404	7
β-strand	405-412	8	1
β-strand	416-424	9	1
α-helix	428-461	34

Chain B: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	25-69	45
β-strand	73-81	9	7
β-strand	85-86	2	8
β-strand	89-94	6	9
α-helix	105-111	7
α-helix	132-141	10
α-helix	149-151	3
α-helix	154-161	8
α-helix	163-164	2
α-helix	165-168	4
β-strand	169-174	6	7
β-strand	177-178	2	7
α-helix	181-183	3
β-strand	184-189	6	9
β-strand	192-197	6	9
α-helix	204-207	4
β-strand	208-209	2	8
β-strand	218-223	6	7
α-helix	226-228	3
α-helix	230-231	2
β-strand	243	1	1
β-strand	245-250	6	9
α-helix	258-261	4
β-strand	263-265	3	9
β-strand	269-281	13	7
β-strand	291	1	10
α-helix	307-323	17
β-strand	326	1	11
α-helix	335	1
β-strand	336	1	11
α-helix	337-338	2
α-helix	339-341	3
α-helix	342-346	5
α-helix	347-355	9
α-helix	358-360	3
α-helix	364-365	2
β-strand	366	1	10
β-strand	368-380	13	7
α-helix	384-394	11
α-helix	398-404	7
β-strand	405-412	8	7
β-strand	416-424	9	7
α-helix	428-445	18
α-helix	447-457	11

Chain C: 21 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	46-69	24
β-strand	73-81	9	4
β-strand	85-86	2	12
β-strand	89-94	6	13
α-helix	105-111	7
α-helix	132-141	10
α-helix	154-161	8
α-helix	163-164	2
α-helix	165-168	4
β-strand	169-174	6	4
β-strand	177-178	2	4
α-helix	181-183	3
β-strand	184-189	6	13
β-strand	192-197	6	13
α-helix	204-207	4
β-strand	208-209	2	12
β-strand	217-223	7	4
α-helix	226-228	3
β-strand	243	1	7
β-strand	245-250	6	13
α-helix	258-261	4
β-strand	263-265	3	13
β-strand	269-281	13	4
β-strand	291	1	14
α-helix	307-323	17
β-strand	326	1	15
α-helix	335	1
β-strand	336	1	15
α-helix	337-338	2
α-helix	339-341	3
α-helix	342-346	5
α-helix	347-356	10
α-helix	358-360	3
α-helix	364-365	2
β-strand	366	1	14
β-strand	368-380	13	4
α-helix	384-394	11
α-helix	398-404	7
β-strand	405-412	8	4
β-strand	416-424	9	4
α-helix	428-450	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Acid-sensing ion channel 1	A, B, C	protein	454	Homo sapiens	P78348 (AlphaFold model)

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

>6L6I_1 Acid-sensing ion channel 1 (chains A, B, C)
GSGGSGLEVLFQGPSTLHGLAHIFSYERLSLKRALWALCFLGSLAVLLCVCTERVQYYFH
YHHVTKLDEVAASQLTFPAVTLCNLNEFRFSQVSKNDLYHAGELLALLNNRYEIPDTQMA
DEKQLEILQDKANFRSFKPKPFNMREFYDRAGHDIRDMLLSCHFRGEVCSAEDFKVVFTR
YGKCYTFNSGRDGRPRLKTMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIH
SQDEPPFIDQLGFGVAPGFQTFVACQEQRLIYLPPPWGTCKAVTMDSDLDFFDSYSITAC
RIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDQEYCVCEMPCNLT
RYGKELSMVKIPSKASAKYLAKKFNKSEQYIGENILVLDIFFEVLNYETIEQKKAYEIAG
LLGDIGGQMGLFIGASILTVLELFDYAYEVIKHK

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3

Primary citation

hASIC1a co-crystallized with Mamb-1. Lei, F., Jian, S. To be published.

Other PDB entries of the same protein (UniProt P78348 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9E4I 2.33 Å, Human ASIC1a at pH 7.5 in complex with MitTx
9E4H 2.61 Å, Human ASIC1a at pH 5.7 with rotated, domain-swapped transmembrane domain
9E4F 2.69 Å, Human ASIC1a at pH 5.7 with domain-swapped transmembrane domain
9E4A 2.74 Å, Human ASIC1a at pH 8.5 with domain-swapped transmembrane domain
9E4K 2.77 Å, Human ASIC1a at pH 8.5, T26V mutation
9E4G 2.8 Å, Human ASIC1a at pH 5.7 with linear transmembrane domain
6L6N 2.86 Å, hASIC1a co-crystallized with Nafamostat
7RNN 2.86 Å, Human ASIC1a-Nb.C1 complex
9E4J 2.87 Å, Human ASIC1a at pH 6.5 in complex with MitTx
9E4B 3.09 Å, Human ASIC1a at pH 7.5 with domain-swapped transmembrane domain
9E4E 3.16 Å, Human ASIC1a at pH 6.5 with linear transmembrane domain
9E4D 3.19 Å, Human ASIC1a at pH 7.5 with linear transmembrane domain

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