2vm4

Structure of Alcaligenes xylosoxidans nitrite reductase in space group R3 - 2 of 2

Method: X-RAY DIFFRACTION Dmax: 82.9 Å Quality: GOOD

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

DISSIMILATORY COPPER-CONTAINING NITRITE REDUCTASE

ACHROMOBACTER XYLOSOXIDANS

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 25–360 Fragment:RESIDUES 25-360 CU COPPER (II) ION × 6 ZN ZINC ION × 3 PG4 TETRAETHYLENE GLYCOL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;pH 6.5 Resolution 1.90 Å R-free 0.214

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 1–336; UniProt 25–360

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 2vm4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2vm4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2vm4
Deposition date deposition_date2008-01-22
Structure title titleStructure of Alcaligenes xylosoxidans nitrite reductase in space group R3 - 2 of 2
Keywords keywordsDENITRIFICATION, NITRITE REDUCTASE, OXIDOREDUCTASE, ORDERED MECHANISM; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.56
Radius of gyration Rg (electron density) rg_electron20.86
Forward intensity I(0) i023001500.00
Molecular weight molecular_weight36527.0 kDa
Excluded volume excluded_volume45673 ų
Envelope volume envelope_volume54962 ų
Hydration-shell volume shell_volume22032 ų
Envelope diameter envelope_diameter84.9
Shell Rg shell_rg27.56
Envelope Rg envelope_rg21.96
Shape Rg shape_rg20.84
Total Rg total_rg21.80
Total atoms total_atoms2566
Residues n_residues334
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 dmax82.9
Rg (real space) rg_real21.58
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real2.3000e+07
I(0) uncertainty (real space) i0_real_error3.1750e+05
Rg (reciprocal space) rg_reciprocal21.57
I(0) (reciprocal space) i0_reciprocal23000000.0000
Solution quality estimate total_estimate0.8004
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.4
Skewness Skewness skewness0.447
Kurtosis Kurtosis kurtosis0.033
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6126000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.533; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.803; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2vm4a1
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_idd2vm4a2
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_id2vm4A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2vm4A02
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)