1cpc

ISOLATION, CRYSTALLIZATION, CRYSTAL STRUCTURE ANALYSIS AND REFINEMENT OF CONSTITUTIVE C-PHYCOCYANIN FROM THE CHROMATICALLY ADAPTING CYANOBACTERIUM FREMYELLA DIPLOSIPHON AT 1.66 ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 98.2 Å Quality: GOOD

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

C-PHYCOCYANIN (ALPHA SUBUNIT)

Fremyella diplosiphon

UniProt P07122

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–162 Not recorded C-PHYCOCYANIN (BETA SUBUNIT) × 1 (P07119) CYC PHYCOCYANOBILIN × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain K; UniProt 1–162 Not recorded C-PHYCOCYANIN (BETA SUBUNIT) × 1 (P07119) CYC PHYCOCYANOBILIN × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–162 Chain K; UniProt 1–162 Not recorded C-PHYCOCYANIN (BETA SUBUNIT) × 6 (P07119) CYC PHYCOCYANOBILIN × 18 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
4 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–162 Not recorded C-PHYCOCYANIN (BETA SUBUNIT) × 3 (P07119) CYC PHYCOCYANOBILIN × 9 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain K; UniProt 1–162 Not recorded C-PHYCOCYANIN (BETA SUBUNIT) × 3 (P07119) CYC PHYCOCYANOBILIN × 9 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
6 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–162 Chain K; UniProt 1–162 Not recorded C-PHYCOCYANIN (BETA SUBUNIT) × 2 (P07119) CYC PHYCOCYANOBILIN × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PHA1_FREDI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–162; UniProt 1–162 Author chain K; PDBConstruct 1–162; UniProt 1–162

C-PHYCOCYANIN (BETA SUBUNIT)

Fremyella diplosiphon

UniProt P07119

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–172 Non-standard monomer:Yes (specific site not provided by mmCIF) C-PHYCOCYANIN (ALPHA SUBUNIT) × 1 (P07122) CYC PHYCOCYANOBILIN × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain L; UniProt 1–172 Non-standard monomer:Yes (specific site not provided by mmCIF) C-PHYCOCYANIN (ALPHA SUBUNIT) × 1 (P07122) CYC PHYCOCYANOBILIN × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–172 Chain L; UniProt 1–172 Non-standard monomer:Yes (specific site not provided by mmCIF) C-PHYCOCYANIN (ALPHA SUBUNIT) × 6 (P07122) CYC PHYCOCYANOBILIN × 18 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
4 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–172 Non-standard monomer:Yes (specific site not provided by mmCIF) C-PHYCOCYANIN (ALPHA SUBUNIT) × 3 (P07122) CYC PHYCOCYANOBILIN × 9 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain L; UniProt 1–172 Non-standard monomer:Yes (specific site not provided by mmCIF) C-PHYCOCYANIN (ALPHA SUBUNIT) × 3 (P07122) CYC PHYCOCYANOBILIN × 9 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å
6 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–172 Chain L; UniProt 1–172 Non-standard monomer:Yes (specific site not provided by mmCIF) C-PHYCOCYANIN (ALPHA SUBUNIT) × 2 (P07122) CYC PHYCOCYANOBILIN × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.66 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name PHB1_FREDI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–172; UniProt 1–172 Author chain L; PDBConstruct 1–172; UniProt 1–172

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1cpc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cpc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cpc
Deposition date deposition_date1990-10-11
Structure title titleISOLATION, CRYSTALLIZATION, CRYSTAL STRUCTURE ANALYSIS AND REFINEMENT OF CONSTITUTIVE C-PHYCOCYANIN FROM THE CHROMATICALLY ADAPTING CYANOBACTERIUM FREMYELLA DIPLOSIPHON AT 1.66 ANGSTROMS RESOLUTION
Keywords keywordsLIGHT HARVESTING PROTEIN; LIGHT HARVESTING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier29.19
Radius of gyration Rg (electron density) rg_electron28.49
Forward intensity I(0) i087458600.00
Molecular weight molecular_weight73839.0 kDa
Excluded volume excluded_volume92455 ų
Envelope volume envelope_volume111450 ų
Hydration-shell volume shell_volume33073 ų
Envelope diameter envelope_diameter105.1
Shell Rg shell_rg35.14
Envelope Rg envelope_rg28.51
Shape Rg shape_rg28.51
Total Rg total_rg29.03
Total atoms total_atoms5191
Residues n_residues666
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax98.2
Rg (real space) rg_real29.18
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real8.7460e+07
I(0) uncertainty (real space) i0_real_error1.2320e+06
Rg (reciprocal space) rg_reciprocal29.19
I(0) (reciprocal space) i0_reciprocal87460000.0000
Solution quality estimate total_estimate0.8898
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary34.5
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.314
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23800000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1cpca_
Class classa — All alpha proteins
Fold Fold folda.1 — Globin-like
Superfamily Superfamily superfamilya.1.1 — Globin-like
Family Family familya.1.1.3 — Phycocyanin-like phycobilisome proteins
Domain ID domain_idd1cpcb_
Class classa — All alpha proteins
Fold Fold folda.1 — Globin-like
Superfamily Superfamily superfamilya.1.1 — Globin-like
Family Family familya.1.1.3 — Phycocyanin-like phycobilisome proteins
Domain ID domain_idd1cpck_
Class classa — All alpha proteins
Fold Fold folda.1 — Globin-like
Superfamily Superfamily superfamilya.1.1 — Globin-like
Family Family familya.1.1.3 — Phycocyanin-like phycobilisome proteins
Domain ID domain_idd1cpcl_
Class classa — All alpha proteins
Fold Fold folda.1 — Globin-like
Superfamily Superfamily superfamilya.1.1 — Globin-like
Family Family familya.1.1.3 — Phycocyanin-like phycobilisome proteins

CATH v4.4 (4 domains)

Domain ID domain_id1cpcA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily20 — Phycocyanins
Domain ID domain_id1cpcB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily20 — Phycocyanins
Domain ID domain_id1cpcK00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily20 — Phycocyanins
Domain ID domain_id1cpcL00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology490 — Globin-like
Homologous superfamily homologous superfamily20 — Phycocyanins

8. Citations (1)

9. Files and Curves (10)