5X61

Crystal structure of Acetylcholinesterase Catalytic Subunit of the Malaria Vector Anopheles Gambiae, 3.4 A

PDB DOI: https://doi.org/10.2210/pdb5X61/pdb

Classification: HYDROLASE
Organism(s): Anopheles gambiae
Expression System: Komagataella pastoris
Mutation(s): No
Membrane Protein: Yes OPM

Deposited: 2017-02-20 Released: 2017-03-15
Deposition Author(s): Han, Q., Robinson, H., Ding, H., Wong, D.M., Lam, P.C.H., Totrov, M.M., Carlier, P.R., Li, J.
Funding Organization(s): National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID), the National Natural Science Foundation of China

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 3.40 Å
R-Value Free: 0.221
R-Value Work: 0.194
R-Value Observed: 0.195

wwPDB Validation 3D Report Full Report

This is version 3.2 of the entry. See complete history.

Literature

Crystal structure of acetylcholinesterase catalytic subunits of the malaria vector Anopheles gambiae

Han, Q., Wong, D.M., Robinson, H., Ding, H., Lam, P.C.H., Totrov, M.M., Carlier, P.R., Li, J.

(2017) Insect Sci

PubMed: 28247978 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1111/1744-7917.12450
Primary Citation of Related Structures:
5X61

Organizational Affiliation

Laboratory of Tropical Veterinary Medicine and Vector Biology, and Hainan Key Laboratory of Sustainable Utilization of Tropical Bioresources, College of Agriculture, Hainan University, Haikou, China.

Macromolecule Content

Total Structure Weight: 126.27 kDa
Atom Count: 8,672
Modelled Residue Count: 1,074
Deposited Residue Count: 1,106
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Acetylcholinesterase	A [auth B], B [auth A]	553	Anopheles gambiae	Mutation(s): 0 Gene Names: Ace, ACE1, ACHE1, AGAP001356 EC: 3.1.1.7 Membrane Entity: Yes
UniProt
Find proteins for Q869C3 (Anopheles gambiae) Explore Q869C3 Go to UniProtKB: Q869C3
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q869C3
Sequence Annotations Expand
Reference Sequence

Oligosaccharides

Help

Entity ID: 2
Molecule	Chains	Length	2D Diagram	Glycosylation	3D Interactions
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose	C, D	2		N-Glycosylation	Interactions Focus chain C Focus chain D Interactions & Density Focus chain C Focus chain D
Glycosylation Resources
GlyTouCan: G79924RM GlyCosmos: G79924RM GlyGen: G79924RM

Small Molecules

Ligands 3 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
EPE Query on EPE Download Ideal Coordinates CCD File SDF format, chain N [auth B] SDF format, chain X [auth A] MOL2 format, chain N [auth B] MOL2 format, chain X [auth A]	N [auth B], X [auth A]	4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID C₈ H₁₈ N₂ O₄ S JKMHFZQWWAIEOD-UHFFFAOYSA-N		Interactions Focus chain N [auth B] Focus chain X [auth A] Interactions & Density Focus chain N [auth B] Focus chain X [auth A]
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain E [auth B] SDF format, chain F [auth B] SDF format, chain G [auth B] SDF format, chain H [auth B] SDF format, chain I [auth B] SDF format, chain J [auth B] SDF format, chain K [auth B] SDF format, chain L [auth B] SDF format, chain O [auth A] SDF format, chain P [auth A] SDF format, chain Q [auth A] SDF format, chain R [auth A] SDF format, chain S [auth A] SDF format, chain T [auth A] SDF format, chain U [auth A] SDF format, chain V [auth A] MOL2 format, chain E [auth B] MOL2 format, chain F [auth B] MOL2 format, chain G [auth B] MOL2 format, chain H [auth B] MOL2 format, chain I [auth B] MOL2 format, chain J [auth B] MOL2 format, chain K [auth B] MOL2 format, chain L [auth B] MOL2 format, chain O [auth A] MOL2 format, chain P [auth A] MOL2 format, chain Q [auth A] MOL2 format, chain R [auth A] MOL2 format, chain S [auth A] MOL2 format, chain T [auth A] MOL2 format, chain U [auth A] MOL2 format, chain V [auth A]	E [auth B] F [auth B] G [auth B] H [auth B] I [auth B] E [auth B], F [auth B], G [auth B], H [auth B], I [auth B], J [auth B], K [auth B], L [auth B], O [auth A], P [auth A], Q [auth A], R [auth A], S [auth A], T [auth A], U [auth A], V [auth A]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain E [auth B] Focus chain F [auth B] Focus chain G [auth B] Focus chain H [auth B] Focus chain I [auth B] Focus chain J [auth B] Focus chain K [auth B] Focus chain L [auth B] Focus chain O [auth A] Focus chain P [auth A] Focus chain Q [auth A] Focus chain R [auth A] Focus chain S [auth A] Focus chain T [auth A] Focus chain U [auth A] Focus chain V [auth A] Interactions & Density Focus chain E [auth B] Focus chain F [auth B] Focus chain G [auth B] Focus chain H [auth B] Focus chain I [auth B] Focus chain J [auth B] Focus chain K [auth B] Focus chain L [auth B] Focus chain O [auth A] Focus chain P [auth A] Focus chain Q [auth A] Focus chain R [auth A] Focus chain S [auth A] Focus chain T [auth A] Focus chain U [auth A] Focus chain V [auth A]
NH4 Query on NH4 Download Ideal Coordinates CCD File SDF format, chain M [auth B] SDF format, chain W [auth A] MOL2 format, chain M [auth B] MOL2 format, chain W [auth A]	M [auth B], W [auth A]	AMMONIUM ION H₄ N QGZKDVFQNNGYKY-UHFFFAOYSA-O		Interactions Focus chain M [auth B] Focus chain W [auth A] Interactions & Density Focus chain M [auth B] Focus chain W [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 3.40 Å
R-Value Free: 0.221
R-Value Work: 0.194
R-Value Observed: 0.195
Space Group: P 6₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 148.723	α = 90
b = 148.723	β = 90
c = 225.796	γ = 120

Software Package:

Software Name	Purpose
REFMAC	refinement
HKL-2000	data reduction
SCALA	data scaling
PHASES	phasing

Structure Validation

View Full Validation Report

Entry History & Funding Information

Deposition Data

Released Date: 2017-03-15

Deposition Author(s):

Funding Organization	Location	Grant Number
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)	United States	AI082581
the National Natural Science Foundation of China	China	31472186

Revision History (Full details and data files)

Version 1.0: 2017-03-15
Type: Initial release
Version 1.1: 2017-10-18
Changes: Author supporting evidence
Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Derived calculations, Structure summary
Version 3.0: 2021-06-02
Changes: Atomic model, Data collection, Derived calculations, Structure summary
Version 3.1: 2022-03-23
Changes: Author supporting evidence, Database references
Version 3.2: 2023-11-22
Changes: Data collection, Refinement description

Prepare Data

Validate Data

Deposit Data

Help and Resources

5X61

Crystal structure of Acetylcholinesterase Catalytic Subunit of the Malaria Vector Anopheles Gambiae, 3.4 A

Crystal structure of acetylcholinesterase catalytic subunits of the malaria vector Anopheles gambiae

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

Expand

Entity ID: 2

Glycosylation Resources

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)