1xi8

Molybdenum cofactor biosynthesis protein from Pyrococcus furiosus Pfu-1657500-001

Method: X-RAY DIFFRACTION

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

Molybdenum cofactor biosynthesis protein

Pyrococcus furiosus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	No other associated polymer	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8U034_PYRFU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 10–403； UniProt 2–395 Author chain B； PDBConstruct 10–403； UniProt 2–395

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	1xi8
Deposition date deposition_date	2004-09-21
Structure title title	Molybdenum cofactor biosynthesis protein from Pyrococcus furiosus Pfu-1657500-001
Keywords keywords	;Structural genomics, Molybdenum cofactor biosynthesis protein, Pyrococcus furiosus, Southeast Collaboratory for Structural Genomics, hyperthermophile, PSI, Protein Structure Initiative, SECSG, unknown function ;; Structural genomics, unknown function
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.

1xi8__assembly_1__model_1

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

Download this curve (.dat)

1xi8__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1xi8__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	25.61 Å
Rg (electron density)	24.28 Å
Total Rg	25.19 Å
Atom count	4034
Residues	534
Excluded volume	73008 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1xi8__assembly_1__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 (1)

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1xi8a1
Class class	b — All beta proteins
Fold Fold fold	b.85 — beta-clip
Superfamily Superfamily superfamily	b.85.6 — MoeA C-terminal domain-like
Family Family family	b.85.6.1 — MoeA C-terminal domain-like

Domain ID domain_id	d1xi8a2
Class class	b — All beta proteins
Fold Fold fold	b.103 — MoeA N-terminal region -like
Superfamily Superfamily superfamily	b.103.1 — MoeA N-terminal region -like
Family Family family	b.103.1.1 — MoeA N-terminal region -like

Domain ID domain_id	d1xi8a3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.57 — Molybdenum cofactor biosynthesis proteins
Superfamily Superfamily superfamily	c.57.1 — Molybdenum cofactor biosynthesis proteins
Family Family family	c.57.1.2 — MoeA central domain-like

Domain ID domain_id	d1xi8b1
Class class	b — All beta proteins
Fold Fold fold	b.85 — beta-clip
Superfamily Superfamily superfamily	b.85.6 — MoeA C-terminal domain-like
Family Family family	b.85.6.1 — MoeA C-terminal domain-like

Domain ID domain_id	d1xi8b2
Class class	b — All beta proteins
Fold Fold fold	b.103 — MoeA N-terminal region -like
Superfamily Superfamily superfamily	b.103.1 — MoeA N-terminal region -like
Family Family family	b.103.1.1 — MoeA N-terminal region -like

Domain ID domain_id	d1xi8b3
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.57 — Molybdenum cofactor biosynthesis proteins
Superfamily Superfamily superfamily	c.57.1 — Molybdenum cofactor biosynthesis proteins
Family Family family	c.57.1.2 — MoeA central domain-like

CATH v4.4 (6 domains)

Domain ID domain_id	1xi8A01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	980 — Molybdenum Cofactor Biosythetic Enzyme; Chain A
Homologous superfamily homologous superfamily	10 — MoaB/Mog-like domain

Domain ID domain_id	1xi8A02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	105 — Molybdopterin biosynthesis moea protein, domain 2
Homologous superfamily homologous superfamily	10 — Molybdopterin biosynthesis moea protein, domain 2

Domain ID domain_id	1xi8A03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	340 — Beta-clip
Homologous superfamily homologous superfamily	10 — MoeA, C-terminal, domain IV

Domain ID domain_id	1xi8B01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	980 — Molybdenum Cofactor Biosythetic Enzyme; Chain A
Homologous superfamily homologous superfamily	10 — MoaB/Mog-like domain

Domain ID domain_id	1xi8B02
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	105 — Molybdopterin biosynthesis moea protein, domain 2
Homologous superfamily homologous superfamily	10 — Molybdopterin biosynthesis moea protein, domain 2

Domain ID domain_id	1xi8B03
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	340 — Beta-clip
Homologous superfamily homologous superfamily	10 — MoeA, C-terminal, domain IV

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Unit-cell length a length_a	63.547 Å
Unit-cell length b length_b	116.599 Å
Unit-cell length c length_c	147.226 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	8

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

Resolution resolution	2.504 Å
Low-resolution limit resolution_low	42.954 Å
R factor r_factor	—
R_work r_work	0.3060
R_free r_free	0.3430

Description description	Molybdenum cofactor biosynthesis protein
Molecular weight formula_weight	44799.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4034

Molybdenum cofactor biosynthesis protein from Pyrococcus furiosus Pfu-1657500-001

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

Molybdenum cofactor biosynthesis protein

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

1xi8__assembly_1__model_1

1xi8__assembly_1__model_1 | I(q)

1xi8__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Source organism organism	Pyrococcus furiosus
NCBI taxonomy ID ncbi_taxonomy_id	2261
Host organism host_organism	Escherichia coli

Molybdenum cofactor biosynthesis protein from Pyrococcus furiosus Pfu-1657500-001

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

Molybdenum cofactor biosynthesis protein

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

1xi8__assembly_1__model_1

1xi8__assembly_1__model_1 | I(q)

1xi8__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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (1)