SAXSdb — 1fm0

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

MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 1

Escherichia coli

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 2 × 1 （P30749） CHLORIDE ION × 3 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 2 × 2 （P30749） CHLORIDE ION × 6 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MOAD_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain D； PDBConstruct 1–81； UniProt 1–81

MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 2

Escherichia coli

UniProt P30749

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 1 × 1 （P30748） CHLORIDE ION × 3 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 4	MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 1 × 2 （P30748） CHLORIDE ION × 6 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MOAE_ECOLI
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–150； UniProt 1–150

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	1fm0
Deposition date deposition_date	2000-08-15
Structure title title	MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)
Keywords keywords	MOLYBDENUM COFACTOR BIOSYNTHESIS, TRANSFERASE; 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.

1fm0__assembly_1__model_1

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

Download this curve (.dat)

1fm0__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1fm0__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	20.29 Å
Rg (electron density)	19.04 Å
Total Rg	19.91 Å
Atom count	1762
Residues	223
Excluded volume	31178 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1fm0__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1fm0__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Description description	MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 1
Molecular weight formula_weight	8764.9 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D
Atom count atom_count	2011

MIKVLFFAQVRELVGTDATEVAADFPTVEALRQHMAAQSDRWALALEDGKLLAAVNQTLVSFDHPLTDGDEVAFFPPVTGG

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 2
Molecular weight formula_weight	17003.0 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

MAETKIVVGPQPFSVGEEYPWLAERDEDGAVVTFTGKVRNHNLGDSVNALTLEHYPGMTEKALAEIVDEARNRWPLGRVTVIHRIGELWPGDEIVFVGVTSAHRSSAFEAGQFIMDYLKTRAPFWKREATPEGDRWVEARESDQQAAKRW

Source Source

Source organism organism	Escherichia coli
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	208

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1fm0d_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamily	d.15.3 — MoaD/ThiS
Family Family family	d.15.3.1 — MoaD

Domain ID domain_id	d1fm0e_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.41 — alpha/beta-Hammerhead
Superfamily Superfamily superfamily	d.41.5 — Molybdopterin synthase subunit MoaE
Family Family family	d.41.5.1 — Molybdopterin synthase subunit MoaE

CATH v4.4 (2 domains)

Domain ID domain_id	1fm0D00
Class class	3 — Alpha Beta
Architecture architecture	10 — Roll
Topology topology	20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily	30 — Beta-grasp domain

Domain ID domain_id	1fm0E00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1170 — Aldehyde Oxidoreductase; domain 3
Homologous superfamily homologous superfamily	40 — Molybdopterin biosynthesis MoaE subunit

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Unit-cell length a length_a	66.029 Å
Unit-cell length b length_b	48.955 Å
Unit-cell length c length_c	76.457 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	107.72 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.450 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.1532
R_work r_work	0.1516
R_free r_free	0.1820

MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)

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

MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 1

State in the Current Structure

Other States of the Same Protein in the Database

MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 2

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

1fm0__assembly_1__model_1

1fm0__assembly_1__model_1 | I(q)

1fm0__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)

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

MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

MOLYBDOPTERIN CONVERTING FACTOR, SUBUNIT 2

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

1fm0__assembly_1__model_1

1fm0__assembly_1__model_1 | I(q)

1fm0__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 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)