SAXSdb — 8sni

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

(S)-hydroxynitrile lyase

Hevea brasiliensis

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	1,2-ETHANEDIOL × 1 SULFATE ION × 2 PROLINE × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	SULFATE ION × 1 PROLINE × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HNL_HEVBR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 35–293； UniProt 1–257 Author chain B； PDBConstruct 35–293； UniProt 1–257

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	8sni
Deposition date deposition_date	2023-04-27
Structure title title	Hydroxynitrile Lyase from Hevea brasiliensis with Forty Mutations
Keywords keywords	Engineered Protein, alpha/beta hydrolase fold, esterase, catalytic promiscuity, LYASE; LYASE
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.

8sni__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

8sni__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

8sni__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	18.14 Å
Rg (electron density)	16.83 Å
Total Rg	17.87 Å
Atom count	2022
Residues	258
Excluded volume	36237 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`8sni__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`8sni__assembly_2__model_1`	monomeric （1）	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 (5)

Entity 1 Entity 1 polymer

Description description	(S)-hydroxynitrile lyase
Molecular weight formula_weight	32793.6 kDa
EC 编号 ec_number	4.1.2.47
Mutation mutation	;I9V, T11G, I12A, I18S, E79H, C81L, L84M, H103L, N104A, S105A, V106F, V118L, L121Y, M122N, F125T, D127N, K129L, Y133F, L146M, K147F, L148F, F150P, T151K, L152F, R154A, E155H, N156K, T159Q, T173V, G176S, Q180M, Q208K, I209G, F210I, L211P, K236M, L237A, Q238M ;
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	4098

MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSMAFAHFVLVHGACHGAWSWHKLKPLLEALGHKVTALDLAASGVDPRQIEEIGSFDEYSEPLLTFLEALPPGEKVILVGHSLGGMNIAIAADKYCEKIAAAVFLAAFLPDTEHCPSYVLDKYNEVTPAENWLDTTFFTYTKDGKEITGMFFGPKFLAHKLYQLCGPEEYELAKMLVRKSSLFMNILAKRPFFTKEGYGSIKKIYVWTDQDKGIPPEFQLWQIENYKPDKVYKVEGGDHMAMLTKTKEIAEILQEVADTYN

Source Source

Source organism organism	Hevea brasiliensis
Common name common_name	rubber tree
NCBI taxonomy ID ncbi_taxonomy_id	3981
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	1

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 non-polymer

Description description	PROLINE
Molecular weight formula_weight	115.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	68

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Unit-cell length a length_a	76.527 Å
Unit-cell length b length_b	81.884 Å
Unit-cell length c length_c	90.929 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	orthorhombic

Resolution resolution	1.990 Å
Low-resolution limit resolution_low	60.850 Å
R factor r_factor	0.2002
R_work r_work	0.1987
R_free r_free	0.2273

Hydroxynitrile Lyase from Hevea brasiliensis with Forty Mutations

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

(S)-hydroxynitrile lyase

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

8sni__assembly_2__model_1

8sni__assembly_2__model_1 | I(q)

8sni__assembly_2__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 (5)

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 water

7. Citations (1)

Hydroxynitrile Lyase from Hevea brasiliensis with Forty Mutations

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

(S)-hydroxynitrile lyase

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

8sni__assembly_2__model_1

8sni__assembly_2__model_1 | I(q)

8sni__assembly_2__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 (5)

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 water

7. Citations (1)