2idf

P. aeruginosa azurin N42C/M64E double mutant, BMME-linked dimer

Method: X-RAY DIFFRACTION Dmax: 77.5 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 21–148 Chain B; UniProt 21–148 Mutation:N42C, M64E CU COPPER (II) ION × 2 NI NICKEL (II) ION × 2 144 TRIS-HYDROXYMETHYL-METHYL-AMMONIUM × 2 OPP 1-[PYRROL-1-YL-2,5-DIONE-METHOXYMETHYL]-PYRROLE-2,5-DIONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;293 K;25% PEG 2000 MME, 10 mM NiCl2, 100 mM Tris/HCl, pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.25 Å R-free 0.261

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 1–128; UniProt 21–148 Author chain B; PDBConstruct 1–128; 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 2idf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2idf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2idf
Deposition date deposition_date2006-09-15
Structure title titleP. aeruginosa azurin N42C/M64E double mutant, BMME-linked dimer
Keywords keywordsprotein crosslinking, cupredoxins, electron transfer, 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_guinier21.51
Radius of gyration Rg (electron density) rg_electron21.06
Forward intensity I(0) i015712700.00
Molecular weight molecular_weight28582.0 kDa
Excluded volume excluded_volume35170 ų
Envelope volume envelope_volume41463 ų
Hydration-shell volume shell_volume17487 ų
Envelope diameter envelope_diameter77.2
Shell Rg shell_rg26.59
Envelope Rg envelope_rg21.52
Shape Rg shape_rg20.97
Total Rg total_rg22.03
Total atoms total_atoms1983
Residues n_residues256
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 dmax77.5
Rg (real space) rg_real21.69
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real1.5710e+07
I(0) uncertainty (real space) i0_real_error2.2710e+05
Rg (reciprocal space) rg_reciprocal21.66
I(0) (reciprocal space) i0_reciprocal15710000.0000
Solution quality estimate total_estimate0.8112
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.564
Kurtosis Kurtosis kurtosis-0.160
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3609000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.619; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.687; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2idfa_
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_idd2idfb_
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_id2idfA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2idfB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins

8. Citations (2)

9. Files and Curves (10)