SAXSdb — 6emi

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Cholinesterase

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	1,2-ETHANEDIOL × 6 DI(HYDROXYETHYL)ETHER × 2 CHLORIDE ION × 10 TRIETHYLENE GLYCOL × 12 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	1,2-ETHANEDIOL × 28 DI(HYDROXYETHYL)ETHER × 6 CHLORIDE ION × 4 TRIETHYLENE GLYCOL × 6 TETRAETHYLENE GLYCOL × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CHLE_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–532； UniProt 29–557 Author chain B； PDBConstruct 4–532； UniProt 29–557

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6emi
Deposition date deposition_date	2017-10-02
Structure title title	Crystal structure of a variant of human butyrylcholinesterase expressed in bacteria.
Keywords keywords	alpha-beta hydrolase, prokaryotic expression, dimeric form, disulfide bond., HYDROLASE; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

6emi__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6emi__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6emi__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	38.70 Å
Rg (electron density)	38.83 Å
Total Rg	39.37 Å
Atom count	8588
Residues	1054
Excluded volume	153240 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6emi__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6emi__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Description description	Cholinesterase
Molecular weight formula_weight	60129.9 kDa
EC 编号 ec_number	3.1.1.8
Mutation mutation	;-3G, -2A, -1M, A7T, S48P, D54G, C66M, Q71T, L110M, I111V, H126P, Q176K, K180D, N188D, K190N, S191R, S215P, F227A, T234M, L236P, Y237E, T250L, L274D, G283S, I305T, N342D, I356V, G360N, V377E, D379E, Q380D, E387D, G390A, D391E, N397F, T406A, F409Y, S410A, W412H, F417Y, D454L, A459E, S466E, V468M, K469R, S489Q, S495P, T508S, Q518H, T523N, 530STOP ;
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	9018

GAMEDDIIITTKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQPLTKWSGIWNATKYANSCMQNIDTSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVMVWIYGGGFQTGTSSLPVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALKWVQDNIAAFGGDPNRVTLFGESAGAASVSLHLLSPGSHPLFTRAILQSGSANAPWAVMSPEEARNRTLNLAKLLGCSRENETEIIKCLRNKDPQEILDNEAFVVPYSTPLSVNFGPTVDGDFLTDMPDTLLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNDSIITRKEFQEGLKVFFPNVSEFGKESILFHYTDWEDEDRPENYRDALAEVVGDYFFICPALEFAKKYAEHGNNAYFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRLNYTKEEEILSREIMRRWANFAKYGNPNETQNNSTQWPVFKPTEQKYLTLNTESSRIMTKLRAQHCRFWNSFFPKV

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	17

Entity 3 Entity 3 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 4 Entity 4 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	7

Entity 5 Entity 5 non-polymer

Description description	TRIETHYLENE GLYCOL
Molecular weight formula_weight	150.2 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 6 Entity 6 non-polymer

Description description	TETRAETHYLENE GLYCOL
Molecular weight formula_weight	194.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 7 Entity 7 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	376

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d6emia_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.0 — automated matches

Domain ID domain_id	d6emib_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	6emiA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

Domain ID domain_id	6emiB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

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Unit-cell length a length_a	159.840 Å
Unit-cell length b length_b	75.170 Å
Unit-cell length c length_c	122.070 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	93.37 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.476 Å
Low-resolution limit resolution_low	65.020 Å
R factor r_factor	0.2237
R_work r_work	0.2220
R_free r_free	0.2553

Crystal structure of a variant of human butyrylcholinesterase expressed in bacteria.

1. Protein Identity and Related Structures Protein Identity & Related Structures

Cholinesterase

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

6emi__assembly_1__model_1

6emi__assembly_1__model_1 | I(q)

6emi__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Crystal structure of a variant of human butyrylcholinesterase expressed in bacteria.

1. Protein Identity and Related Structures Protein Identity & Related Structures

Cholinesterase

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

6emi__assembly_1__model_1

6emi__assembly_1__model_1 | I(q)

6emi__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (7)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)