2iwe

Structure of a cavity mutant (H117G) of Pseudomonas aeruginosa azurin

Method: X-RAY DIFFRACTION Dmax: 93.8 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 J; UniProt 21–148 Mutation:YES ZN ZINC ION × 2 2IH 1,1'-HEXANE-1,6-DIYLBIS(1H-IMIDAZOLE) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;100 MM TRIS-HCL PH 8.5 AND 20% (W/V) POLYETHYLENE GLYCOL (PEG) 8000 Resolution 2.83 Å R-free 0.233
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 21–148 Chain G; UniProt 21–148 Mutation:YES ZN ZINC ION × 2 2IH 1,1'-HEXANE-1,6-DIYLBIS(1H-IMIDAZOLE) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;100 MM TRIS-HCL PH 8.5 AND 20% (W/V) POLYETHYLENE GLYCOL (PEG) 8000 Resolution 2.83 Å R-free 0.233

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 1–128; UniProt 21–148 Author chain D; PDBConstruct 1–128; UniProt 21–148 Author chain G; PDBConstruct 1–128; UniProt 21–148 Author chain J; 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 2iwe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2iwe
Deposition date deposition_date2006-06-29
Structure title titleStructure of a cavity mutant (H117G) of Pseudomonas aeruginosa azurin
Keywords keywordsBLUE COPPER PROTEIN, REDOX PROTEIN, METAL-BINDING, ELECTRON TRANSPORT, AZURIN, TRANSPORT, PERIPLASMIC; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.97
Radius of gyration Rg (electron density) rg_electron28.36
Forward intensity I(0) i054662500.00
Molecular weight molecular_weight56149.0 kDa
Excluded volume excluded_volume69435 ų
Envelope volume envelope_volume89818 ų
Hydration-shell volume shell_volume26512 ų
Envelope diameter envelope_diameter100.2
Shell Rg shell_rg35.61
Envelope Rg envelope_rg27.93
Shape Rg shape_rg28.35
Total Rg total_rg29.08
Total atoms total_atoms3908
Residues n_residues512
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 dmax93.8
Rg (real space) rg_real28.93
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real5.4660e+07
I(0) uncertainty (real space) i0_real_error7.6130e+05
Rg (reciprocal space) rg_reciprocal28.95
I(0) (reciprocal space) i0_reciprocal54660000.0000
Solution quality estimate total_estimate0.8887
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.6
Skewness Skewness skewness0.181
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10050000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.896

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_idd2iwea_
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_idd2iwed_
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_idd2iweg_
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_idd2iwej_
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_id2iweA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2iweD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2iweG00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2iweJ00
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)