1cc3

PURPLE CUA CENTER

Method: X-RAY DIFFRACTION Dmax: 61.9 Å Quality: EXCELLENT

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

PROTEIN (CUA AZURIN)

Pseudomonas aeruginosa

UniProt P00282

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 21–148 Not recorded CU COPPER (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.1;pH 5.1 Resolution 1.65 Å R-free 0.263
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 21–148 Not recorded CU COPPER (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.1;pH 5.1 Resolution 1.65 Å R-free 0.263

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.

110 other PDB entries and 269 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AZUR_PSEAE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–130; UniProt 21–148 Author chain B; PDBConstruct 1–130; UniProt 21–148

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 1cc3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cc3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cc3
Deposition date deposition_date1999-03-03
Structure title titlePURPLE CUA CENTER
Keywords keywordsCOPPER-A, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.14
Radius of gyration Rg (electron density) rg_electron19.34
Forward intensity I(0) i015884400.00
Molecular weight molecular_weight28592.0 kDa
Excluded volume excluded_volume35150 ų
Envelope volume envelope_volume41707 ų
Hydration-shell volume shell_volume18415 ų
Envelope diameter envelope_diameter67.2
Shell Rg shell_rg24.97
Envelope Rg envelope_rg19.20
Shape Rg shape_rg19.27
Total Rg total_rg20.30
Total atoms total_atoms1980
Residues n_residues260
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 dmax61.9
Rg (real space) rg_real20.06
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real1.5880e+07
I(0) uncertainty (real space) i0_real_error1.8770e+05
Rg (reciprocal space) rg_reciprocal20.08
I(0) (reciprocal space) i0_reciprocal15880000.0000
Solution quality estimate total_estimate0.9143
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.140
Kurtosis Kurtosis kurtosis-0.616
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2117000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1cc3a_
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.1 — Plastocyanin/azurin-like
Domain ID domain_idd1cc3b_
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.1 — Plastocyanin/azurin-like

CATH v4.4 (2 domains)

Domain ID domain_id1cc3A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1cc3B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins

8. Citations (1)

9. Files and Curves (10)