2jbw

Crystal Structure of the 2,6-dihydroxy-pseudo-oxynicotine Hydrolase.

Method: X-RAY DIFFRACTION

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

2,6-DIHYDROXY-PSEUDO-OXYNICOTINE HYDROLASE

ARTHROBACTER NICOTINOVORANS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	SODIUM ION × 2 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	SODIUM ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q93NG6_ARTNI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 15–379； UniProt 1–365 Author chain B； PDBConstruct 15–379； UniProt 1–365 Author chain C； PDBConstruct 15–379； UniProt 1–365 Author chain D； PDBConstruct 15–379； UniProt 1–365

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	2jbw
Deposition date deposition_date	2006-12-14
Structure title title	Crystal Structure of the 2,6-dihydroxy-pseudo-oxynicotine Hydrolase.
Keywords keywords	;HYDROLASE, ALPHA/BETA HYDROLASE, META-CLEAVAGE PATHWAY, RETRO- FRIEDEL- CRAFTS ACYLATION, NICOTINE DEGRADATION, HYPOTHETICAL PROTEIN, PLASMID, CATALYTIC TRIAD, C-C BOND CLEAVAGE ;; 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.

2jbw__assembly_1__model_1

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

Download this curve (.dat)

2jbw__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2jbw__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.37 Å
Rg (electron density)	26.71 Å
Total Rg	27.37 Å
Atom count	5657
Residues	699
Excluded volume	100950 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2jbw__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2jbw__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 (3)

Entity 1 Entity 1 polymer

Description description	2,6-DIHYDROXY-PSEUDO-OXYNICOTINE HYDROLASE
Molecular weight formula_weight	43861.5 kDa
EC 编号 ec_number	3.7.1.-
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	12210

ASMTGGQQMGRDPGMTVTSQVKPEDEMDNWGRLILDGVSYSDMVGARDRPKEITWFDYWMSLANEYEQEAERKVALGHDLSAGELLMSAALCAQYAQFLWFDERRQKGQARKVELYQKAAPLLSPPAERHELVVDGIPMPVYVRIPEGPGPHPAVIMLGGLESTKEESFQMENLVLDRGMATATFDGPGQGEMFEYKRIAGDYEKYTSAVVDLLTKLEAIRNDAIGVLGRSLGGNYALKSAACEPRLAACISWGGFSDLDYWDLETPLTKESWKYVSKVDTLEEARLHVHAALETRDVLSQIACPTYILHGVHDEVPLSFVDTVLELVPAEHLNLVVEKDGDHCCHNLGIRPRLEMADWLYDVLVAGKKVAPTMKGWPLEHHHHHH

Source Source

Source organism organism	ARTHROBACTER NICOTINOVORANS
NCBI taxonomy ID ncbi_taxonomy_id	29320
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	964

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d2jbwa1
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.69.1.41 — 2,6-dihydropseudooxynicotine hydrolase-like

Domain ID domain_id	d2jbwa2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2jbwb1
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.69.1.41 — 2,6-dihydropseudooxynicotine hydrolase-like

Domain ID domain_id	d2jbwb2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2jbwc1
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.69.1.41 — 2,6-dihydropseudooxynicotine hydrolase-like

Domain ID domain_id	d2jbwc2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2jbwd1
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.69.1.41 — 2,6-dihydropseudooxynicotine hydrolase-like

Domain ID domain_id	d2jbwd2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (8 domains)

Domain ID domain_id	2jbwA01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily	110 — acylaminoacyl peptidase

Domain ID domain_id	2jbwA02
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	2jbwB01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily	110 — acylaminoacyl peptidase

Domain ID domain_id	2jbwB02
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	2jbwC01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily	110 — acylaminoacyl peptidase

Domain ID domain_id	2jbwC02
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	2jbwD01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily	110 — acylaminoacyl peptidase

Domain ID domain_id	2jbwD02
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	90.570 Å
Unit-cell length b length_b	57.020 Å
Unit-cell length c length_c	152.697 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	103.35 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.1830
R_work r_work	0.1810
R_free r_free	0.2380

Crystal Structure of the 2,6-dihydroxy-pseudo-oxynicotine Hydrolase.

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

2,6-DIHYDROXY-PSEUDO-OXYNICOTINE HYDROLASE

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

2jbw__assembly_1__model_1

2jbw__assembly_1__model_1 | I(q)

2jbw__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)

Crystal Structure of the 2,6-dihydroxy-pseudo-oxynicotine Hydrolase.

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

2,6-DIHYDROXY-PSEUDO-OXYNICOTINE HYDROLASE

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

2jbw__assembly_1__model_1

2jbw__assembly_1__model_1 | I(q)

2jbw__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)