6L6N: HASIC1a co-crystallized with Nafamostat

hASIC1a co-crystallized with Nafamostat. Determined by X-ray diffraction at 2.86 Å resolution. Released 13 Jan 2021.

Method: X-ray diffraction
Resolution: 2.86 Å
Organism: Homo sapiens
Chains: 3
Atoms: 9,786
Mol. weight: 156.34 kDa
Ligands: NAG, NDG
Released: 13 Jan 2021

Explore 6L6N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6L6N contains 75 α-helices and 65 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, 21 β-strands

Element	Residues	Length	Sheet
α-helix	51-61	11
α-helix	63-70	8
β-strand	73-81	9	1
β-strand	85-86	2	2
β-strand	89-94	6	3
α-helix	100-102	3
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	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
α-helix	214-216	3
β-strand	218-223	6	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
β-strand	299	1	6
β-strand	302	1	6
α-helix	307-323	17
β-strand	326	1	7
α-helix	335	1
β-strand	336	1	7
α-helix	337-338	2
α-helix	339-341	3
α-helix	342-346	5
α-helix	347-355	9
α-helix	364-365	2
β-strand	366	1	5
β-strand	368-380	13	1
α-helix	384-393	10
α-helix	398-404	7
β-strand	405-424	20	1
α-helix	429-448	20

Chain B: 26 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	49-61	13
α-helix	63-70	8
β-strand	73-81	9	8
β-strand	85-86	2	9
β-strand	89-94	6	10
α-helix	100-102	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	8
β-strand	177-178	2	8
α-helix	181-183	3
β-strand	184-189	6	10
β-strand	192-197	6	10
α-helix	204-207	4
β-strand	208-209	2	9
α-helix	214-216	3
β-strand	218-223	6	8
α-helix	226-228	3
α-helix	230-231	2
β-strand	243	1	1
β-strand	245-250	6	10
α-helix	258-261	4
β-strand	263-265	3	10
β-strand	269-281	13	8
β-strand	291	1	11
β-strand	299	1	12
β-strand	302	1	12
α-helix	307-323	17
β-strand	326	1	13
α-helix	335	1
β-strand	336	1	13
α-helix	337-338	2
α-helix	339-341	3
α-helix	342-346	5
α-helix	347-355	9
α-helix	364-365	2
β-strand	366	1	11
β-strand	368-380	13	8
α-helix	387-393	7
α-helix	398-404	7
β-strand	405-424	20	8
α-helix	429-438	10
α-helix	445-448	4

Chain C: 25 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	49-61	13
α-helix	63-70	8
β-strand	73-81	9	4
β-strand	85-86	2	14
β-strand	89-94	6	15
β-strand	99	1	16
α-helix	100-102	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	4
β-strand	177-178	2	4
α-helix	181-183	3
β-strand	184-189	6	15
β-strand	192-197	6	15
α-helix	204-207	4
β-strand	208-209	2	14
α-helix	214-216	3
β-strand	218-223	6	4
α-helix	226-228	3
β-strand	229	1	16
α-helix	230-231	2
β-strand	243	1	8
β-strand	245-250	6	15
α-helix	258-261	4
β-strand	263-265	3	15
β-strand	269-281	13	4
β-strand	291	1	17
β-strand	299	1	18
β-strand	302	1	18
α-helix	307-323	17
β-strand	326	1	19
α-helix	335	1
β-strand	336	1	19
α-helix	337-338	2
α-helix	339-341	3
α-helix	342-346	5
α-helix	347-355	9
α-helix	364-365	2
β-strand	366	1	17
β-strand	368-380	13	4
α-helix	387-393	7
α-helix	398-404	7
β-strand	405-424	20	4
α-helix	429-446	18

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

>6L6N_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	4
NDG	2-acetamido-2-deoxy-alpha-D-glucopyranose	C8 H15 N O6	1

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

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
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
6L6I 3.24 Å, hASIC1a co-crystallized with Mamb-1

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