SAXSdb — 1nnh

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

asparaginyl-tRNA synthetase-related peptide

Pyrococcus furiosus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	SODIUM ION × 1 water × 1	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	SODIUM ION × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8TZN6_PYRFU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–294； UniProt 1–294

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	1nnh
Deposition date deposition_date	2003-01-13
Structure title title	Hypothetical protein from Pyrococcus furiosus Pfu-1801964
Keywords keywords	;Pyrococcus furiosus, asparaginyl-tRNA synthetase, structural genomics, PSI, Protein Structure Initiative, Southeast Collaboratory for Structural Genomics, 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.

1nnh__assembly_1__model_1

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

Download this curve (.dat)

1nnh__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1nnh__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.83 Å
Rg (electron density)	18.87 Å
Total Rg	19.93 Å
Atom count	2341
Residues	293
Excluded volume	42184 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1nnh__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1nnh__assembly_2__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 (3)

Entity 1 Entity 1 polymer

Description description	asparaginyl-tRNA synthetase-related peptide
Molecular weight formula_weight	34098.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2502

MNAVEIISREISPTLDIQTKILEYMTDFFVKEGFKWLLPVIISPITDPLWPDPAGEGMEPAEVEIYGVKMRLTHSMILHKQLAIAMGLKKIFVLSPNIRLESRQKDDGRHAYEFTQLDFEVERAKMEDIMRLIERLVYGLFRKAEEWTGREFPKTKRFEVFEYSEVLEEFGSDEKASQEMEEPFWIINIPREFYDREVDGFWRNYDLILPYGYGEVASGGEREWEYEKIVAKIRKAGLNEDSFRPYLEIAKAGKLKPSAGAGIGVERLVRFIVGAKHIAEVQPFPRIPGIPAVI

Source Source

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

Entity 2 Entity 2 non-polymer

Description description	SODIUM ION
Molecular weight formula_weight	23.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	148

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1nnha_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.104 — Class II aaRS and biotin synthetases
Superfamily Superfamily superfamily	d.104.1 — Class II aaRS and biotin synthetases
Family Family family	d.104.1.1 — Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain

CATH v4.4 (1 domains)

Domain ID domain_id	1nnhA00
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	930 — BirA Bifunctional Protein; domain 2
Homologous superfamily homologous superfamily	10 — Bira Bifunctional Protein; Domain 2

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Unit-cell length a length_a	68.529 Å
Unit-cell length b length_b	68.529 Å
Unit-cell length c length_c	150.684 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	I 41
Space-group number int_tables_number	80
Crystal system crystal_system	—

Resolution resolution	1.650 Å
Low-resolution limit resolution_low	62.020 Å
R factor r_factor	0.1720
R_work r_work	0.1710
R_free r_free	0.1910

Hypothetical protein from Pyrococcus furiosus Pfu-1801964

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

asparaginyl-tRNA synthetase-related peptide

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

1nnh__assembly_1__model_1

1nnh__assembly_1__model_1 | I(q)

1nnh__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Hypothetical protein from Pyrococcus furiosus Pfu-1801964

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

asparaginyl-tRNA synthetase-related peptide

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

1nnh__assembly_1__model_1

1nnh__assembly_1__model_1 | I(q)

1nnh__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)