3fsa

Pseudomonas aeruginosa Azurin with mutated metal-binding loop sequence (CAAHAAM); chemically reduced.

Method: X-RAY DIFFRACTION Dmax: 46.5 Å Quality: GOOD

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

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 CU1 COPPER (I) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.1M potassium thiocyanate, 30% PEG 2000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 0.98 Å R-free 0.135

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 270 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 1–125; 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 3fsa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3fsa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3fsa
Deposition date deposition_date2009-01-09
Structure title titlePseudomonas aeruginosa Azurin with mutated metal-binding loop sequence (CAAHAAM); chemically reduced.
Keywords keywordscupredoxin fold, metal-binding, protein-protein interaction, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.89
Radius of gyration Rg (electron density) rg_electron13.66
Forward intensity I(0) i03666130.00
Molecular weight molecular_weight13053.0 kDa
Excluded volume excluded_volume16122 ų
Envelope volume envelope_volume18191 ų
Hydration-shell volume shell_volume11473 ų
Envelope diameter envelope_diameter46.0
Shell Rg shell_rg19.24
Envelope Rg envelope_rg13.95
Shape Rg shape_rg13.62
Total Rg total_rg14.92
Total atoms total_atoms908
Residues n_residues122
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 dmax46.5
Rg (real space) rg_real14.80
Rg uncertainty (real space) rg_real_error0.16
I(0) (real space) i0_real3.6660e+06
I(0) uncertainty (real space) i0_real_error3.3000e+04
Rg (reciprocal space) rg_reciprocal14.81
I(0) (reciprocal space) i0_reciprocal3666000.0000
Solution quality estimate total_estimate0.7535
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.7
Skewness Skewness skewness0.134
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha579800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.997; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3fsaa_
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 (1 domains)

Domain ID domain_id3fsaA00
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)