6fog

X-ray structure of homo sapiens Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) in complex with inhibitor oxalate at 1.94A resolution.

Method: X-RAY DIFFRACTION

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

Acylpyruvase FAHD1, mitochondrial

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	MAGNESIUM ION × 3 OXALATE ION × 2 CHLORIDE ION × 1 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	MAGNESIUM ION × 3 OXALATE ION × 2 CHLORIDE ION × 1 water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	MAGNESIUM ION × 3 OXALATE ION × 2 CHLORIDE ION × 1 water × 2	Consistent with protein count
4	Protein homooligomer	Homooligomer	Protein 2	MAGNESIUM ION × 3 OXALATE ION × 2 CHLORIDE ION × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FAHD1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–224； UniProt 1–224 Author chain B； PDBConstruct 1–224； UniProt 1–224 Author chain C； PDBConstruct 1–224； UniProt 1–224 Author chain D； PDBConstruct 1–224； UniProt 1–224 Author chain E； PDBConstruct 1–224； UniProt 1–224 Author chain F； PDBConstruct 1–224； UniProt 1–224 Author chain G； PDBConstruct 1–224； UniProt 1–224 Author chain H； PDBConstruct 1–224； UniProt 1–224

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	6fog
Deposition date deposition_date	2018-02-07
Structure title title	X-ray structure of homo sapiens Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) in complex with inhibitor oxalate at 1.94A resolution.
Keywords keywords	FAHD 1, Fumarylacetoacetate hydrolase domain containing protein 1, oxalate, inhibitor, hydrolase/lyase, hydrolase-lyase complex; hydrolase/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.

6fog__assembly_1__model_1

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

Download this curve (.dat)

6fog__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

6fog__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.20 Å
Rg (electron density)	21.12 Å
Total Rg	22.00 Å
Atom count	3398
Residues	434
Excluded volume	61173 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`6fog__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`6fog__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`6fog__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`6fog__assembly_4__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 (5)

Entity 1 Entity 1 polymer

Description description	Acylpyruvase FAHD1, mitochondrial
Molecular weight formula_weight	24875.0 kDa
EC 编号 ec_number	3.7.1.5,4.1.1.3
Source method src_method	man
Copy count entity_count	8

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,G,F,D,B,C,H,E
Atom count atom_count	14391

MGIMAASRPLSRFWEWGKNIVCVGRNYADHVREMRSAVLSEPVLFLKPSTAYAPEGSPILMPAYTRNLHHELELGVVMGKRCRAVPEAAAMDYVGGYALCLDMTARDVQDECKKKGLPWTLAKSFTASCPVSAFVPKEKIPDPHKLKLWLKVNGELRQEGETSSMIFSIPYIISYVSKIITLEEGDIILTGTPKGVGPVKENDEIEAGIHGLVSMTFKVEKPEY

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	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	12

Entity 3 Entity 3 non-polymer

Description description	OXALATE ION
Molecular weight formula_weight	88.0 kDa
Source method src_method	syn
Copy count entity_count	8

Entity 4 Entity 4 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	841

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6. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_id	d6foga_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d6fogb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d6fogc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d6fogd_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d6foge_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d6fogf_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d6fogg_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

Domain ID domain_id	d6fogh_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.177 — FAH
Superfamily Superfamily superfamily	d.177.1 — FAH
Family Family family	d.177.1.1 — FAH

CATH v4.4 (8 domains)

Domain ID domain_id	6fogA00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	6fogB00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	6fogC00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	6fogD00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	6fogE00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	6fogF00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	6fogG00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

Domain ID domain_id	6fogH00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	850 — Fumarylacetoacetate hydrolase; domain 2
Homologous superfamily homologous superfamily	10 — Fumarylacetoacetase-like, C-terminal domain

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Unit-cell length a length_a	75.984 Å
Unit-cell length b length_b	116.679 Å
Unit-cell length c length_c	125.753 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	89.94 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

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

Resolution resolution	1.940 Å
Low-resolution limit resolution_low	85.530 Å
R factor r_factor	0.1824
R_work r_work	0.1809
R_free r_free	0.2083

X-ray structure of homo sapiens Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) in complex with inhibitor oxalate at 1.94A resolution.

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

Acylpyruvase FAHD1, mitochondrial

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

6fog__assembly_1__model_1

6fog__assembly_1__model_1 | I(q)

6fog__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)

X-ray structure of homo sapiens Fumarylacetoacetate hydrolase domain containing protein 1 (FAHD1) in complex with inhibitor oxalate at 1.94A resolution.

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

Acylpyruvase FAHD1, mitochondrial

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

6fog__assembly_1__model_1

6fog__assembly_1__model_1 | I(q)

6fog__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) 16 domains

SCOP 2.08 (8 domains)

CATH v4.4 (8 domains)

7. Citations (1)