4bww

Crystal structure of spin labelled azurin T21R1.

Method: X-RAY DIFFRACTION Dmax: 103.6 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 21–148 Chain B; UniProt 21–148 Chain C; UniProt 21–148 Chain D; UniProt 21–148 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 4 GOL GLYCEROL × 8 NO3 NITRATE ION × 5 SO4 SULFATE ION × 5 X-RAY DIFFRACTION X-ray crystallization conditions:2.14 M AMMONIUM SULFATE, 0.28 M AMMONIUM NITRATE, 0.1 M SODIUM CACODYLATE PH 6.0 Resolution 1.48 Å R-free 0.210

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 4–131; UniProt 21–148 Author chain B; PDBConstruct 4–131; UniProt 21–148 Author chain C; PDBConstruct 4–131; UniProt 21–148 Author chain D; PDBConstruct 4–131; 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 4bww

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4bww
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4bww
Deposition date deposition_date2013-07-04
Structure title titleCrystal structure of spin labelled azurin T21R1.
Keywords keywordsELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.08
Radius of gyration Rg (electron density) rg_electron27.97
Forward intensity I(0) i061778300.00
Molecular weight molecular_weight58302.0 kDa
Excluded volume excluded_volume71529 ų
Envelope volume envelope_volume86389 ų
Hydration-shell volume shell_volume27466 ų
Envelope diameter envelope_diameter107.3
Shell Rg shell_rg32.99
Envelope Rg envelope_rg28.51
Shape Rg shape_rg27.90
Total Rg total_rg28.66
Total atoms total_atoms4037
Residues n_residues508
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 dmax103.6
Rg (real space) rg_real28.38
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real6.1780e+07
I(0) uncertainty (real space) i0_real_error8.8960e+05
Rg (reciprocal space) rg_reciprocal28.29
I(0) (reciprocal space) i0_reciprocal61770000.0000
Solution quality estimate total_estimate0.8054
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.8
Skewness Skewness skewness0.610
Kurtosis Kurtosis kurtosis0.050
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12550000.0000
Real-space data points n_real_points57
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: 0.634; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4bwwa_
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_idd4bwwb_
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_idd4bwwc_
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_idd4bwwd_
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 (4 domains)

Domain ID domain_id4bwwA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id4bwwB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id4bwwC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id4bwwD00
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)