1bq5

NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS GIFU 1051

Method: X-RAY DIFFRACTION Dmax: 83.8 Å Quality: GOOD

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

NITRITE REDUCTASE

OrganismNot specified

UniProt O68601

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 19–360 Not recorded CU COPPER (II) ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;pH 8.5 Resolution 2.05 Å R-free 0.226

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.

36 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O68601_ALCXX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–342; UniProt 19–360

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 1bq5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bq5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bq5
Deposition date deposition_date1998-08-21
Structure title titleNITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS GIFU 1051
Keywords keywordsOXIDOREDUCTASE, NITRITE REDUCTASE, CUPROPROTEIN; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.67
Radius of gyration Rg (electron density) rg_electron20.91
Forward intensity I(0) i022626300.00
Molecular weight molecular_weight36190.0 kDa
Excluded volume excluded_volume45247 ų
Envelope volume envelope_volume55187 ų
Hydration-shell volume shell_volume22050 ų
Envelope diameter envelope_diameter86.1
Shell Rg shell_rg27.73
Envelope Rg envelope_rg22.07
Shape Rg shape_rg20.89
Total Rg total_rg21.89
Total atoms total_atoms2546
Residues n_residues333
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 dmax83.8
Rg (real space) rg_real21.68
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real2.2630e+07
I(0) uncertainty (real space) i0_real_error3.2950e+05
Rg (reciprocal space) rg_reciprocal21.68
I(0) (reciprocal space) i0_reciprocal22630000.0000
Solution quality estimate total_estimate0.7953
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.428
Kurtosis Kurtosis kurtosis-0.022
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5959000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.526; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.758; Smooth: 0.998

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_idd1bq5a1
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.3 — Multidomain cupredoxins
Domain ID domain_idd1bq5a2
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.3 — Multidomain cupredoxins

CATH v4.4 (2 domains)

Domain ID domain_id1bq5A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id1bq5A02
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)