1dq9

COMPLEX OF CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG-COA

Method: X-RAY DIFFRACTION

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

PROTEIN (HMG-COA REDUCTASE)

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 4	3-HYDROXY-3-METHYLGLUTARYL-COENZYME A × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HMDH_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–467； UniProt 422–888 Author chain B； PDBConstruct 1–467； UniProt 422–888 Author chain C； PDBConstruct 1–467； UniProt 422–888 Author chain D； PDBConstruct 1–467； UniProt 422–888

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	1dq9
Deposition date deposition_date	1999-12-30
Structure title title	COMPLEX OF CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG-COA
Keywords keywords	OXIDOREDUCTASE, CHOLESTEROL BIOSYNTHESIS, HMG-COA, NADPH; OXIDOREDUCTASE
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.

1dq9__assembly_1__model_1

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

Download this curve (.dat)

1dq9__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1dq9__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	33.82 Å
Rg (electron density)	33.39 Å
Total Rg	33.83 Å
Atom count	12351
Residues	1630
Excluded volume	220090 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1dq9__assembly_1__model_1`	tetrameric （4）	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 (2)

Entity 1 Entity 1 polymer

Description description	PROTEIN (HMG-COA REDUCTASE)
Molecular weight formula_weight	50021.5 kDa
EC 编号 ec_number	1.1.1.34
Mutation mutation	YES
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	12351

GAMASSVLVTQEPEIELPREPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKTA

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	3-HYDROXY-3-METHYLGLUTARYL-COENZYME A
Molecular weight formula_weight	906.6 kDa
Source method src_method	syn
Copy count entity_count	4

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6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1dq9a1
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	d1dq9a4
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	d1dq9b1
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	d1dq9b4
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	d1dq9c1
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	d1dq9c4
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	d1dq9d1
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	d1dq9d4
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

CATH v4.4 (12 domains)

Domain ID domain_id	1dq9A01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3270 — HMGR, N-terminal domain
Homologous superfamily homologous superfamily	10 — HMGR, N-terminal domain

Domain ID domain_id	1dq9A02
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	1dq9A03
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	1dq9B01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3270 — HMGR, N-terminal domain
Homologous superfamily homologous superfamily	10 — HMGR, N-terminal domain

Domain ID domain_id	1dq9B02
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	1dq9B03
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	1dq9C01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3270 — HMGR, N-terminal domain
Homologous superfamily homologous superfamily	10 — HMGR, N-terminal domain

Domain ID domain_id	1dq9C02
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	1dq9C03
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	1dq9D01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	3270 — HMGR, N-terminal domain
Homologous superfamily homologous superfamily	10 — HMGR, N-terminal domain

Domain ID domain_id	1dq9D02
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	1dq9D03
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

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Unit-cell length a length_a	74.580 Å
Unit-cell length b length_b	171.200 Å
Unit-cell length c length_c	80.370 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	116.59 °
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	2.800 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.2070
R_work r_work	0.2070
R_free r_free	0.2470

COMPLEX OF CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG-COA

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

PROTEIN (HMG-COA 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

1dq9__assembly_1__model_1

1dq9__assembly_1__model_1 | I(q)

1dq9__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

CATH v4.4 (12 domains)

7. Citations (1)

COMPLEX OF CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG-COA

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

PROTEIN (HMG-COA 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

1dq9__assembly_1__model_1

1dq9__assembly_1__model_1 | I(q)

1dq9__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 (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

CATH v4.4 (12 domains)

7. Citations (1)