SAXSdb — 2c6r

▼

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

DNA-BINDING STRESS RESPONSE PROTEIN, DPS FAMILY

DEINOCOCCUS RADIODURANS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 12	FE (III) ION × 60 CHLORIDE ION × 12 water × 12	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9RZN1_DEIRA
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–211； UniProt 31–241

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	2c6r
Deposition date deposition_date	2005-11-11
Structure title title	FE-SOAKED CRYSTAL STRUCTURE OF THE DPS92 FROM DEINOCOCCUS RADIODURANS
Keywords keywords	DPS, DEINOCOCCUS, RADIODURANS, DNA-BINDING PROTEIN, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

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.

2c6r__assembly_1__model_1

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

Download this curve (.dat)

2c6r__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2c6r__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	36.61 Å
Rg (electron density)	35.64 Å
Total Rg	36.10 Å
Atom count	15888
Residues	1992
Excluded volume	280890 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2c6r__assembly_1__model_1`	dodecameric （12）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	DNA-BINDING STRESS RESPONSE PROTEIN, DPS FAMILY
Molecular weight formula_weight	23289.7 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	1474

NGVPSTNVNTPAPNTGQSTAQNTNTASPLPYNRATTLPAAGTEDLKKSVQALQNTLTELQALQLQTKQAHWNVSGTLWYTLHELLQDHYEGISKFADDVAERQLSVGASSDGRAITIVAASRLPEIPGGFLDDAQVIQFFTYQYETVGQRIHQRVGDVEKVDPTTANLLQEVEHIIEKYQWQMRAFLQNTPTDPNTGFDINNGKPVPLRGR

Source Source

Source organism organism	DEINOCOCCUS RADIODURANS
NCBI taxonomy ID ncbi_taxonomy_id	243230
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	FE (III) ION
Molecular weight formula_weight	55.8 kDa
Source method src_method	syn
Copy count entity_count	5

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	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	135

▼

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	2c6rA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1260 — Ferritin
Homologous superfamily homologous superfamily	10 — Ferritin, core subunit, four-helix bundle

▶

Unit-cell length a length_a	88.965 Å
Unit-cell length b length_b	88.965 Å
Unit-cell length c length_c	88.965 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	12

Space group space_group	P 2 3
Space-group number int_tables_number	195
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	89.090 Å
R factor r_factor	0.1880
R_work r_work	0.1880
R_free r_free	—

FE-SOAKED CRYSTAL STRUCTURE OF THE DPS92 FROM DEINOCOCCUS RADIODURANS

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

DNA-BINDING STRESS RESPONSE PROTEIN, DPS FAMILY

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

2c6r__assembly_1__model_1

2c6r__assembly_1__model_1 | I(q)

2c6r__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)

FE-SOAKED CRYSTAL STRUCTURE OF THE DPS92 FROM DEINOCOCCUS RADIODURANS

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

DNA-BINDING STRESS RESPONSE PROTEIN, DPS FAMILY

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

2c6r__assembly_1__model_1

2c6r__assembly_1__model_1 | I(q)

2c6r__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 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)