2bp8

M144Q Structure of nitrite reductase from Alcaligenes xylosoxidans

Method: X-RAY DIFFRACTION Dmax: 110.2 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 Mutation:YES CU COPPER (II) ION × 6 ZN ZINC ION × 15 SO4 SULFATE ION × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å R-free 0.189
2 Protein homooligomer Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 25–360 Mutation:YES CU COPPER (II) ION × 6 ZN ZINC ION × 15 SO4 SULFATE ION × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å R-free 0.189

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 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O68601_ALCXX
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–336; UniProt 25–360 Author chain B; 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 2bp8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2bp8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2bp8
Deposition date deposition_date2005-04-18
Structure title titleM144Q Structure of nitrite reductase from Alcaligenes xylosoxidans
Keywords keywordsOXIDOREDUCTASE, DENTRIFICATION, NITRITE REDUCTASE, M168Q, MUTANT, ELECTRON TRANSFER, NITRATE ASSIMILATION, PERIPLASMIC; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.86
Radius of gyration Rg (electron density) rg_electron33.88
Forward intensity I(0) i088344000.00
Molecular weight molecular_weight73185.0 kDa
Excluded volume excluded_volume90649 ų
Envelope volume envelope_volume123250 ų
Hydration-shell volume shell_volume31740 ų
Envelope diameter envelope_diameter119.3
Shell Rg shell_rg38.00
Envelope Rg envelope_rg34.27
Shape Rg shape_rg33.88
Total Rg total_rg34.20
Total atoms total_atoms5111
Residues n_residues670
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 dmax110.2
Rg (real space) rg_real34.08
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real8.8340e+07
I(0) uncertainty (real space) i0_real_error1.4870e+06
Rg (reciprocal space) rg_reciprocal33.95
I(0) (reciprocal space) i0_reciprocal88330000.0000
Solution quality estimate total_estimate0.8351
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.1
Skewness Skewness skewness0.440
Kurtosis Kurtosis kurtosis-0.570
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17060000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.713; Smooth: 0.651

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_idd2bp8a1
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_idd2bp8a2
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_idd2bp8b1
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_idd2bp8b2
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 (4 domains)

Domain ID domain_id2bp8A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2bp8A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2bp8B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2bp8B02
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)