2jfd

Structure of the MAT domain of human FAS

Method: X-RAY DIFFRACTION

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

FATTY ACID SYNTHASE

HOMO SAPIENS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
3	Protein monomer	Monomer	Protein 1	water × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FAS_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 24–425； UniProt 422–823 Author chain B； PDBConstruct 24–425； UniProt 422–823 Author chain C； PDBConstruct 24–425； UniProt 422–823 Author chain D； PDBConstruct 24–425； UniProt 422–823

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	2jfd
Deposition date deposition_date	2007-01-31
Structure title title	Structure of the MAT domain of human FAS
Keywords keywords	TRANSFERASE, OXIDOREDUCTASE, LIPID SYNTHESIS, FATTY ACID BIOSYNTHESIS; TRANSFERASE
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.

2jfd__assembly_1__model_1

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

Download this curve (.dat)

2jfd__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2jfd__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	22.64 Å
Rg (electron density)	21.81 Å
Total Rg	22.59 Å
Atom count	2929
Residues	404
Excluded volume	52074 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2jfd__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2jfd__assembly_2__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`2jfd__assembly_3__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`2jfd__assembly_4__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 (2)

Entity 1 Entity 1 polymer

Description description	FATTY ACID SYNTHASE
Molecular weight formula_weight	46736.7 kDa
EC 编号 ec_number	2.3.1.85
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	11392

MHHHHHHSSGVDLGTENLYFQSMRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAVLAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPA

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 BL21(DE3)

Entity 2 Entity 2 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	15

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6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (20 domains)

Domain ID domain_id	d2jfda1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.390 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like
Superfamily Superfamily superfamily	d.390.1 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like
Family Family family	d.390.1.1 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like

Domain ID domain_id	d2jfda2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.19 — FabD/lysophospholipase-like
Superfamily Superfamily superfamily	c.19.1 — FabD/lysophospholipase-like
Family Family family	c.19.1.1 — FabD-like

Domain ID domain_id	d2jfda3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.19 — FabD/lysophospholipase-like
Superfamily Superfamily superfamily	c.19.1 — FabD/lysophospholipase-like
Family Family family	c.19.1.1 — FabD-like

Domain ID domain_id	d2jfda4
Class class	j — Peptides
Fold Fold fold	j.134 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like
Superfamily Superfamily superfamily	j.134.1 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like
Family Family family	j.134.1.1 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like

Domain ID domain_id	d2jfda5
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2jfdb1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.390 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like
Superfamily Superfamily superfamily	d.390.1 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like
Family Family family	d.390.1.1 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like

Domain ID domain_id	d2jfdb2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.19 — FabD/lysophospholipase-like
Superfamily Superfamily superfamily	c.19.1 — FabD/lysophospholipase-like
Family Family family	c.19.1.1 — FabD-like

Domain ID domain_id	d2jfdb3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.19 — FabD/lysophospholipase-like
Superfamily Superfamily superfamily	c.19.1 — FabD/lysophospholipase-like
Family Family family	c.19.1.1 — FabD-like

Domain ID domain_id	d2jfdb4
Class class	j — Peptides
Fold Fold fold	j.134 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like
Superfamily Superfamily superfamily	j.134.1 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like
Family Family family	j.134.1.1 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like

Domain ID domain_id	d2jfdb5
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2jfdc1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.390 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like
Superfamily Superfamily superfamily	d.390.1 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like
Family Family family	d.390.1.1 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like

Domain ID domain_id	d2jfdc2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.19 — FabD/lysophospholipase-like
Superfamily Superfamily superfamily	c.19.1 — FabD/lysophospholipase-like
Family Family family	c.19.1.1 — FabD-like

Domain ID domain_id	d2jfdc3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.19 — FabD/lysophospholipase-like
Superfamily Superfamily superfamily	c.19.1 — FabD/lysophospholipase-like
Family Family family	c.19.1.1 — FabD-like

Domain ID domain_id	d2jfdc4
Class class	j — Peptides
Fold Fold fold	j.134 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like
Superfamily Superfamily superfamily	j.134.1 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like
Family Family family	j.134.1.1 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like

Domain ID domain_id	d2jfdc5
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d2jfdd1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.390 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like
Superfamily Superfamily superfamily	d.390.1 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like
Family Family family	d.390.1.1 — KS-to-AT linker domain from 6-deoxyerythronolide B synthase (DEBS)-like

Domain ID domain_id	d2jfdd2
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.19 — FabD/lysophospholipase-like
Superfamily Superfamily superfamily	c.19.1 — FabD/lysophospholipase-like
Family Family family	c.19.1.1 — FabD-like

Domain ID domain_id	d2jfdd3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.19 — FabD/lysophospholipase-like
Superfamily Superfamily superfamily	c.19.1 — FabD/lysophospholipase-like
Family Family family	c.19.1.1 — FabD-like

Domain ID domain_id	d2jfdd4
Class class	j — Peptides
Fold Fold fold	j.134 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like
Superfamily Superfamily superfamily	j.134.1 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like
Family Family family	j.134.1.1 — C-terminal linker of 6-deoxyerythronolide B synthase (DEBS)-like

Domain ID domain_id	d2jfdd5
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (12 domains)

Domain ID domain_id	2jfdA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	3290 —

Domain ID domain_id	2jfdA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	366 — Malonyl-Coenzyme A Acyl Carrier Protein; domain 2
Homologous superfamily homologous superfamily	10 — Malonyl-Coenzyme A Acyl Carrier Protein, domain 2

Domain ID domain_id	2jfdA03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	250 — Malonyl-CoA ACP transacylase, ACP-binding

Domain ID domain_id	2jfdB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	3290 —

Domain ID domain_id	2jfdB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	366 — Malonyl-Coenzyme A Acyl Carrier Protein; domain 2
Homologous superfamily homologous superfamily	10 — Malonyl-Coenzyme A Acyl Carrier Protein, domain 2

Domain ID domain_id	2jfdB03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	250 — Malonyl-CoA ACP transacylase, ACP-binding

Domain ID domain_id	2jfdC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	3290 —

Domain ID domain_id	2jfdC02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	366 — Malonyl-Coenzyme A Acyl Carrier Protein; domain 2
Homologous superfamily homologous superfamily	10 — Malonyl-Coenzyme A Acyl Carrier Protein, domain 2

Domain ID domain_id	2jfdC03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	250 — Malonyl-CoA ACP transacylase, ACP-binding

Domain ID domain_id	2jfdD01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	3290 —

Domain ID domain_id	2jfdD02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	366 — Malonyl-Coenzyme A Acyl Carrier Protein; domain 2
Homologous superfamily homologous superfamily	10 — Malonyl-Coenzyme A Acyl Carrier Protein, domain 2

Domain ID domain_id	2jfdD03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily	250 — Malonyl-CoA ACP transacylase, ACP-binding

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Unit-cell length a length_a	85.980 Å
Unit-cell length b length_b	92.690 Å
Unit-cell length c length_c	259.870 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	16

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

Resolution resolution	2.810 Å
Low-resolution limit resolution_low	45.220 Å
R factor r_factor	0.2150
R_work r_work	0.2120
R_free r_free	0.2730

Structure of the MAT domain of human FAS

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

FATTY ACID SYNTHASE

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

2jfd__assembly_1__model_1

2jfd__assembly_1__model_1 | I(q)

2jfd__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 water

6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (20 domains)

CATH v4.4 (12 domains)

7. Citations (1)

Structure of the MAT domain of human FAS

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

FATTY ACID SYNTHASE

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

2jfd__assembly_1__model_1

2jfd__assembly_1__model_1 | I(q)

2jfd__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 water

6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (20 domains)

CATH v4.4 (12 domains)

7. Citations (1)