SAXSdb — 4i6w

▼

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

3-hydroxy-3-methylglutaryl-coenzyme A reductase

Pseudomonas mevalonii

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	(3S)-3-hydroxy-3-methyl-5-sulfanylpentanoic acid × 2 SULFATE ION × 4 GLYCEROL × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MVAA_PSEMV
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–428； UniProt 1–428 Author chain B； PDBConstruct 1–428； UniProt 1–428

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	4i6w
Deposition date deposition_date	2012-11-30
Structure title title	3-hydroxy-3-methylglutaryl (HMG) Coenzyme-A reductase complexed with thiomevalonate
Keywords keywords	Oxidoreductase; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

4i6w__assembly_1__model_1

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

Download this curve (.dat)

4i6w__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4i6w__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	26.91 Å
Rg (electron density)	25.66 Å
Total Rg	26.47 Å
Atom count	5613
Residues	749
Excluded volume	99938 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4i6w__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	3-hydroxy-3-methylglutaryl-coenzyme A reductase
Molecular weight formula_weight	45641.2 kDa
EC 编号 ec_number	1.1.1.88
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	6340

MSLDSRLPAFRNLSPAARLDHIGQLLGLSHDDVSLLANAGALPMDIANGMIENVIGTFELPYAVASNFQINGRDVLVPLVVEEPSIVAAASYMAKLARANGGFTTSSSAPLMHAQVQIVGIQDPLNARLSLLRRKDEIIELANRKDQLLNSLGGGCRDIEVHTFADTPRGPMLVAHLIVDVRDAMGANTVNTMAEAVAPLMEAITGGQVRLRILSNLADLRLARAQVRITPQQLETAEFSGEAVIEGILDAYAFAAVDPYRAATHNKGIMNGIDPLIVATGNDWRAVEAGAHAYACRSGHYGSLTTWEKDNNGHLVGTLEMPMPVGLVGGATKTHPLAQLSLRILGVKTAQALAEIAVAVGLAQNLGAMRALATEGIQRGHMALHARNIAVVAGARGDEVDWVARQLVEYHDVRADRAVALLKQKRGQ

Source Source

Source organism organism	Pseudomonas mevalonii
NCBI taxonomy ID ncbi_taxonomy_id	32044
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	(3S)-3-hydroxy-3-methyl-5-sulfanylpentanoic acid
Molecular weight formula_weight	164.2 kDa
Source method src_method	syn
Copy count entity_count	2

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	4

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 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	701

▼

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d4i6wa1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.179 — Substrate-binding domain of HMG-CoA reductase
Superfamily Superfamily superfamily	d.179.1 — Substrate-binding domain of HMG-CoA reductase
Family Family family	d.179.1.1 — Substrate-binding domain of HMG-CoA reductase

Domain ID domain_id	d4i6wa2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.20 — NAD-binding domain of HMG-CoA reductase
Family Family family	d.58.20.1 — NAD-binding domain of HMG-CoA reductase

Domain ID domain_id	d4i6wb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.179 — Substrate-binding domain of HMG-CoA reductase
Superfamily Superfamily superfamily	d.179.1 — Substrate-binding domain of HMG-CoA reductase
Family Family family	d.179.1.1 — Substrate-binding domain of HMG-CoA reductase

Domain ID domain_id	d4i6wb2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.58 — Ferredoxin-like
Superfamily Superfamily superfamily	d.58.20 — NAD-binding domain of HMG-CoA reductase
Family Family family	d.58.20.1 — NAD-binding domain of HMG-CoA reductase

CATH v4.4 (4 domains)

Domain ID domain_id	4i6wA01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	770 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2

Domain ID domain_id	4i6wA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	420 — Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain

Domain ID domain_id	4i6wB01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	770 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — 3-hydroxy-3-methylglutaryl-coenzyme A Reductase; Chain A, domain 2

Domain ID domain_id	4i6wB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	420 — Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain

▶

Unit-cell length a length_a	226.100 Å
Unit-cell length b length_b	226.100 Å
Unit-cell length c length_c	226.100 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	96

Space group space_group	I 41 3 2
Space-group number int_tables_number	214
Crystal system crystal_system	—

Resolution resolution	1.660 Å
Low-resolution limit resolution_low	38.780 Å
R factor r_factor	0.1939
R_work r_work	0.1933
R_free r_free	0.2182

3-hydroxy-3-methylglutaryl (HMG) Coenzyme-A reductase complexed with thiomevalonate

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

3-hydroxy-3-methylglutaryl-coenzyme A reductase

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

4i6w__assembly_1__model_1

4i6w__assembly_1__model_1 | I(q)

4i6w__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 (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

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)

3-hydroxy-3-methylglutaryl (HMG) Coenzyme-A reductase complexed with thiomevalonate

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

3-hydroxy-3-methylglutaryl-coenzyme A reductase

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

4i6w__assembly_1__model_1

4i6w__assembly_1__model_1 | I(q)

4i6w__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 (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

6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

CATH v4.4 (4 domains)

7. Citations (1)