1hw8

COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH COMPACTIN (ALSO KNOWN AS MEVASTATIN)

Method: X-RAY DIFFRACTION

▼

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

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	;(3R,5R)-3,5-dihydroxy-7-[(1S,2S,8S,8aR)-2-methyl-8-{[(2S)-2-methylbutanoyl]oxy}-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]h eptanoic acid ; × 4 ADENOSINE-5'-DIPHOSPHATE × 2 water × 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 5–467； UniProt 426–888 Author chain B； PDBConstruct 5–467； UniProt 426–888 Author chain C； PDBConstruct 5–467； UniProt 426–888 Author chain D； PDBConstruct 5–467； UniProt 426–888

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1hw8
Deposition date deposition_date	2001-01-09
Structure title title	COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH COMPACTIN (ALSO KNOWN AS MEVASTATIN)
Keywords keywords	protein-inhibitor complex, 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.

1hw8__assembly_1__model_1

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

Download this curve (.dat)

1hw8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1hw8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	33.49 Å
Rg (electron density)	32.84 Å
Total Rg	33.35 Å
Atom count	11735
Residues	1559
Excluded volume	209450 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1hw8__assembly_1__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	HMG-COA REDUCTASE
Molecular weight formula_weight	50021.5 kDa
EC 编号 ec_number	1.1.1.34
Mutation mutation	M485I
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	12022

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	;(3R,5R)-3,5-dihydroxy-7-[(1S,2S,8S,8aR)-2-methyl-8-{[(2S)-2-methylbutanoyl]oxy}-1,2,6,7,8,8a-hexahydronaphthalen-1-yl]h eptanoic acid ;
Molecular weight formula_weight	408.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	ADENOSINE-5'-DIPHOSPHATE
Molecular weight formula_weight	427.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	287

▼

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d1hw8a1
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	d1hw8a2
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	d1hw8b1
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	d1hw8b2
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	d1hw8c1
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	d1hw8c2
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	d1hw8d1
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	d1hw8d2
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	1hw8A01
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	1hw8A02
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	1hw8A03
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	1hw8B01
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	1hw8B02
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	1hw8B03
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	1hw8C01
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	1hw8C02
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	1hw8C03
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	1hw8D01
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	1hw8D02
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	1hw8D03
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	73.827 Å
Unit-cell length b length_b	173.003 Å
Unit-cell length c length_c	75.177 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	118.38 °
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	43.130 Å
R factor r_factor	—
R_work r_work	0.1910
R_free r_free	0.2230

COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH COMPACTIN (ALSO KNOWN AS MEVASTATIN)

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

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

1hw8__assembly_1__model_1

1hw8__assembly_1__model_1 | I(q)

1hw8__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

CATH v4.4 (12 domains)

7. Citations (1)

COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH COMPACTIN (ALSO KNOWN AS MEVASTATIN)

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

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

1hw8__assembly_1__model_1

1hw8__assembly_1__model_1 | I(q)

1hw8__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 (4)

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 water

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

CATH v4.4 (12 domains)

7. Citations (1)