SAXSdb — 2ccy

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

CYTOCHROME C

Phaeospirillum molischianum

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	HEME C × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CYCP_RHOMO
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–128； UniProt 1–128 Author chain B； PDBConstruct 1–128； UniProt 1–128

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	2ccy
Deposition date deposition_date	1985-08-27
Structure title title	STRUCTURE OF FERRICYTOCHROME C(PRIME) FROM RHODOSPIRILLUM MOLISCHIANUM AT 1.67 ANGSTROMS RESOLUTION
Keywords keywords	ELECTRON TRANSPORT (HEME PROTEIN); ELECTRON TRANSPORT (HEME PROTEIN)
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.

2ccy__assembly_1__model_1

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

Download this curve (.dat)

2ccy__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2ccy__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	19.47 Å
Rg (electron density)	18.37 Å
Total Rg	19.27 Å
Atom count	1944
Residues	254
Excluded volume	34872 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2ccy__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 (3)

Entity 1 Entity 1 polymer

Description description	CYTOCHROME C
Molecular weight formula_weight	13439.4 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	2146

QQSKPEDLLKLRQGLMQTLKSQWVPIAGFAAGKADLPADAAQRAENMAMVAKLAPIGWAKGTEALPNGETKPEAFGSKSAEFLEGWKALATESTKLAAAAKAGPDALKAQAAATGKVCKACHEEFKQD

Source Source

Source organism organism	Phaeospirillum molischianum
NCBI taxonomy ID ncbi_taxonomy_id	1083

Entity 2 Entity 2 non-polymer

Description description	HEME C
Molecular weight formula_weight	618.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	194

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2ccya_
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.3 — Cytochromes
Family Family family	a.24.3.2 — Cytochrome c'-like

Domain ID domain_id	d2ccyb_
Class class	a — All alpha proteins
Fold Fold fold	a.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamily	a.24.3 — Cytochromes
Family Family family	a.24.3.2 — Cytochrome c'-like

CATH v4.4 (2 domains)

Domain ID domain_id	2ccyA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	10 — Cytochrome c/b562

Domain ID domain_id	2ccyB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily	10 — Cytochrome c/b562

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7. Citations (8)

;Structure of ferricytochrome c' from Rhodospirillum molischianum at 1.67 A resolution. ;

J.Mol.Biol. (1985)

PMID: 3005592 · DOI: 10.1016/0022-2836(85)90135-4 PRIMARY

Lattice Mobility and Anomalous Temperature Factor Behaviour in Cytochrome C(Prime)

Nature (1985)

Correlations between Structural and Spectroscopic Properties of the High-Spin Heme Protein Cytochrome C(Prime)

Biochemistry (1982)

Crystallographic Structure of Rhodospirillum Molischianum Ferricytochrome C(Prime) at 2.5 Angstroms Resolution

J.Mol.Biol. (1981)

On the Evolutionary Relationship of the 4-Alpha-Helical Heme Proteins. The Comparison of Cytochrome B562 and Cytochrome C(Prime)

J.Biol.Chem. (1981)

Structural and Functional Diversity in 4-Alpha-Helical Proteins

Nature (1980)

Structure of Cytochrome C(Prime). A Dimeric, High-Spin Haem Protein

Nature (1980)

Preliminary Crystallographic Data for Cytochromes C(Prime) of Rhodopseudomonas Capsulata and Rhodospirillum Molischianum

J.Mol.Biol. (1977)

Unit-cell length a length_a	56.580 Å
Unit-cell length b length_b	72.330 Å
Unit-cell length c length_c	75.440 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	1.670 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

STRUCTURE OF FERRICYTOCHROME C(PRIME) FROM RHODOSPIRILLUM MOLISCHIANUM AT 1.67 ANGSTROMS RESOLUTION

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

CYTOCHROME C

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

2ccy__assembly_1__model_1

2ccy__assembly_1__model_1 | I(q)

2ccy__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (8)

STRUCTURE OF FERRICYTOCHROME C(PRIME) FROM RHODOSPIRILLUM MOLISCHIANUM AT 1.67 ANGSTROMS RESOLUTION

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

CYTOCHROME C

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

2ccy__assembly_1__model_1

2ccy__assembly_1__model_1 | I(q)

2ccy__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

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) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (8)