7EGR: Co-crystal structure of Ac-AChBPP

Co-crystal structure of Ac-AChBPP in complex with RgIA. Determined by X-ray diffraction at 2.5 Å resolution. Released 6 Apr 2022.

Method: X-ray diffraction
Resolution: 2.5 Å
Organisms: Aplysia californica, Conus regius
Chains: 18
Atoms: 17,680
Mol. weight: 245.85 kDa
Ligands: MG
Released: 6 Apr 2022

Explore 7EGR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7EGR contains 66 α-helices and 156 β-strands across 17 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: 6 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	21-27	7
α-helix	28-32	5
α-helix	35-37	3
β-strand	46-61	16	1
β-strand	66-83	18	1
α-helix	86-89	4
β-strand	94-98	5	1
α-helix	99-101	3
β-strand	107-109	3	2
β-strand	112	1	1
α-helix	115-116	2
β-strand	117-118	2	1
β-strand	123-127	5	1
β-strand	129-134	6	1
β-strand	137-143	7	1
β-strand	155-163	9	2
β-strand	171-174	4	1
β-strand	179	1	2
β-strand	181	1	1
β-strand	191-203	13	2
β-strand	212-223	12	2

Chain B: 6 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	21-31	11
α-helix	35-37	3
β-strand	46-61	16	3
β-strand	66-83	18	3
α-helix	86-89	4
β-strand	94-98	5	3
α-helix	99-101	3
β-strand	107-109	3	4
β-strand	112	1	3
α-helix	115-116	2
β-strand	117-118	2	3
β-strand	123-127	5	3
β-strand	129-134	6	3
β-strand	137-143	7	3
β-strand	155-163	9	4
β-strand	171-174	4	3
β-strand	179	1	4
α-helix	180	1
β-strand	181	1	3
β-strand	192-203	12	4
β-strand	212-222	11	4

Chain C: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	21-31	11
α-helix	35-37	3
β-strand	46-61	16	5
β-strand	66-83	18	5
α-helix	86-88	3
β-strand	94-98	5	5
α-helix	99-101	3
β-strand	107-109	3	6
β-strand	112	1	5
α-helix	115-116	2
β-strand	117-118	2	5
β-strand	123-127	5	5
β-strand	129-134	6	5
β-strand	137-143	7	5
β-strand	155-163	9	6
β-strand	171-174	4	5
β-strand	179	1	6
β-strand	181	1	5
β-strand	192-203	12	6
β-strand	212-222	11	6

Chain D: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	20-27	8
α-helix	28-32	5
α-helix	35-37	3
β-strand	46-61	16	7
β-strand	66-83	18	7
β-strand	94-98	5	7
α-helix	99-101	3
β-strand	107-109	3	8
β-strand	112	1	7
α-helix	115-116	2
β-strand	117-118	2	7
β-strand	123-127	5	7
β-strand	129-134	6	7
β-strand	137-143	7	7
β-strand	155-163	9	8
β-strand	171-175	5	7
β-strand	179	1	8
β-strand	181	1	7
β-strand	191-203	13	8
β-strand	212-223	12	8

Chain E: 6 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	20-27	8
α-helix	28-32	5
α-helix	35-37	3
β-strand	41	1	9
β-strand	44	1	9
β-strand	46-61	16	10
β-strand	66-83	18	10
α-helix	86-89	4
β-strand	94-98	5	10
α-helix	99-101	3
β-strand	107-109	3	11
β-strand	112	1	10
β-strand	117-118	2	10
β-strand	123-127	5	10
β-strand	129-134	6	10
β-strand	137-143	7	10
β-strand	155-163	9	11
β-strand	171-174	4	10
β-strand	179	1	11
β-strand	181	1	10
β-strand	192-203	12	11
α-helix	211	1
β-strand	212-222	11	11

Chain F: 5 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	20-31	12
α-helix	35-37	3
β-strand	41	1	12
β-strand	44	1	12
β-strand	46-61	16	13
β-strand	66-83	18	13
α-helix	86-89	4
β-strand	94-98	5	13
α-helix	99-101	3
β-strand	107-109	3	14
β-strand	112	1	13
α-helix	115-116	2
β-strand	117-118	2	13
β-strand	123-127	5	13
β-strand	129-134	6	13
β-strand	137-143	7	13
β-strand	155-163	9	14
β-strand	171-175	5	13
β-strand	179	1	14
β-strand	181	1	13
β-strand	192-203	12	14
β-strand	212-222	11	14

Chain G: 6 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	20-32	13
β-strand	46-61	16	15
β-strand	66-78	13	15
α-helix	80-82	3
α-helix	86-88	3
β-strand	94-98	5	15
α-helix	99-101	3
β-strand	107-109	3	16
β-strand	112	1	15
α-helix	115-116	2
β-strand	117-118	2	15
β-strand	123-127	5	15
β-strand	131-134	4	15
β-strand	137-143	7	15
β-strand	155-163	9	16
β-strand	171-175	5	15
β-strand	179	1	16
α-helix	180	1
β-strand	181	1	15
β-strand	191-203	13	16
β-strand	212-223	12	16

Chain H: 5 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	20-27	8
α-helix	28-32	5
α-helix	35-37	3
β-strand	46-61	16	17
β-strand	66-83	18	17
α-helix	86-88	3
β-strand	94-98	5	17
α-helix	99-101	3
β-strand	107-109	3	18
β-strand	112	1	17
β-strand	117-118	2	17
β-strand	123-127	5	17
β-strand	129-134	6	17
β-strand	137-143	7	17
β-strand	155-163	9	18
β-strand	171-174	4	17
β-strand	179	1	18
β-strand	181	1	17
β-strand	191-203	13	18
β-strand	212-223	12	18

6 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
Soluble acetylcholine receptor	A, D, G, H, I, J	protein	206	Aplysia californica	Q8WSF8 (AlphaFold model)
Soluble acetylcholine receptor	B, C	protein	204	Aplysia californica	Q8WSF8 (AlphaFold model)
Soluble acetylcholine receptor	E, F	protein	205	Aplysia californica	Q8WSF8 (AlphaFold model)
RgIA	K, L, M, N, O, P, Q, R	protein	13	Conus regius	P0C1D0 (AlphaFold model)

Sequence of entity 1 (A, D, G, H, I, J), FASTA

>7EGR_1 Soluble acetylcholine receptor (chains A, D, G, H, I, J)
SQANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVKVDSSTNEVDLVYYEQQRWK
LNSLMWDPNEYGNITDFRTSAADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQ
RLSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYASSKYEILSATQ
TRQVQHYSCCPEPYIDVNLVVKFRER

Sequence of entity 2 (B, C), FASTA

>7EGR_2 Soluble acetylcholine receptor (chains B, C)
QANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVKVDSSTNEVDLVYYEQQRWKL
NSLMWDPNEYGNITDFRTSAADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQR
LSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYASSKYEILSATQT
RQVQHYSCCPEPYIDVNLVVKFRE

Sequence of entity 3 (E, F), FASTA

>7EGR_3 Soluble acetylcholine receptor (chains E, F)
SQANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVKVDSSTNEVDLVYYEQQRWK
LNSLMWDPNEYGNITDFRTSAADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQ
RLSFMCDPTGVDSEEGVTCAVKFGSWVYSGFEIDLKTDTDQVDLSSYYASSKYEILSATQ
TRQVQHYSCCPEPYIDVNLVVKFRE

Sequence of entity 4 (K, L, M, N, O, P, Q, R), FASTA

>7EGR_4 RgIA (chains K, L, M, N, O, P, Q, R)
GCCSDPRCRYRCR

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	10

Primary citation

Co-crystal structure of Ac-AChBPP in complex with RgIA. Wang, X.Q., Pan, S., Fan, Y.X. et al. To be published.

Other PDB entries of the same protein (UniProt Q8WSF8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6T9R 1.72 Å, Aplysia californica AChBP in complex with a cytisine derivative
2WN9 1.75 Å, Crystal structure of Aplysia ACHBP in complex with 4-0H-DMXBA
2PGZ 1.76 Å, Crystal structure of Cocaine bound to an ACh-Binding Protein
2WNJ 1.8 Å, Crystal structure of aplysia achbp in complex with dmxba
8QTL 1.85 Å, Aplysia californica acetylcholine-binding protein in complex with Spiroimine (-)-4 S
2Y7Y 1.9 Å, Aplysia californica achbp in apo state
4XHE 1.9 Å, Crystal Structure of A-AChBP in complex with pinnatoxin A
4ZK4 1.9 Å, Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica…
2XYS 1.91 Å, Crystal structure of Aplysia californica AChBP in complex with strychnine
5TVC 1.93 Å, Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica…
3C84 1.94 Å, Crystal structure of a complex of AChBP from aplysia californica and the neonicotinoid…
2YMD 1.96 Å, Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with serotonin…

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