SAXSdb — 2ams

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

High potential iron-sulfur protein

Allochromatium vinosum

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	SULFATE ION × 2 IRON/SULFUR CLUSTER × 1 GLYCEROL × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	HIP_THETI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–83； UniProt 1–83

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	2ams
Deposition date deposition_date	2005-08-10
Structure title title	Structure of the oxidized Hipip from thermochromatium tepidum at 1.4 angstrom resolution
Keywords keywords	iron-sulfur protein, electron transport; ELECTRON TRANSPORT
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.

2ams__assembly_1__model_1

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

Download this curve (.dat)

2ams__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2ams__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	12.48 Å
Rg (electron density)	11.54 Å
Total Rg	12.61 Å
Atom count	640
Residues	83
Excluded volume	11251 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2ams__assembly_1__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 (5)

Entity 1 Entity 1 polymer

Description description	High potential iron-sulfur protein
Molecular weight formula_weight	8793.9 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	731

AAPANAVTADDPTAIALKYNQDATKSERVAAARPGLPPEEQHCANCQFMQANVGEGDWKGCQLFPGKLINVNGWCASWTLKAG

Source Source

Source organism organism	Allochromatium vinosum
NCBI taxonomy ID ncbi_taxonomy_id	1049
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	IRON/SULFUR CLUSTER
Molecular weight formula_weight	351.6 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	78

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d2amsa_
Class class	g — Small proteins
Fold Fold fold	g.35 — HIPIP (high potential iron protein)
Superfamily Superfamily superfamily	g.35.1 — HIPIP (high potential iron protein)
Family Family family	g.35.1.1 — HIPIP (high potential iron protein)

CATH v4.4 (1 domains)

Domain ID domain_id	2amsA00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	490 — High-Potential Iron-Sulfur Protein; Chain A
Homologous superfamily homologous superfamily	10 — High potential iron-sulphur protein

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Unit-cell length a length_a	23.460 Å
Unit-cell length b length_b	46.550 Å
Unit-cell length c length_c	59.050 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	4

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

Resolution resolution	1.400 Å
Low-resolution limit resolution_low	36.550 Å
R factor r_factor	0.1572
R_work r_work	0.1566
R_free r_free	0.1944

Structure of the oxidized Hipip from thermochromatium tepidum at 1.4 angstrom resolution

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

High potential iron-sulfur 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

2ams__assembly_1__model_1

2ams__assembly_1__model_1 | I(q)

2ams__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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)

Structure of the oxidized Hipip from thermochromatium tepidum at 1.4 angstrom resolution

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

High potential iron-sulfur 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

2ams__assembly_1__model_1

2ams__assembly_1__model_1 | I(q)

2ams__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) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

7. Citations (1)