1an9

D-AMINO ACID OXIDASE COMPLEX WITH O-AMINOBENZOATE

Method: X-RAY DIFFRACTION Dmax: 111.5 Å Quality: GOOD

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

D-AMINO ACID OXIDASE

Sus scrofa

UniProt P00371

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 1–340 Chain B; UniProt 1–340 Not recorded FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 BE2 2-AMINOBENZOIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.3;PROTEIN WAS CRYSTALLIZED FROM 120MM SODIUM ACETATE, 60MM SODIUM CITRATE, 30% PEG4000, pH 6.3 Resolution 2.50 Å R-free 0.260

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.

12 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OXDA_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–340; UniProt 1–340 Author chain B; PDBConstruct 1–340; UniProt 1–340

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 1an9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1an9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1an9
Deposition date deposition_date1997-06-28
Structure title titleD-AMINO ACID OXIDASE COMPLEX WITH O-AMINOBENZOATE
Keywords keywordsFAD, OXIDASE, D-AMINO ACID, OXIDOREDUCTASE, FLAVOPROTEIN; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.40
Radius of gyration Rg (electron density) rg_electron29.94
Forward intensity I(0) i096807700.00
Molecular weight molecular_weight78986.0 kDa
Excluded volume excluded_volume99057 ų
Envelope volume envelope_volume114920 ų
Hydration-shell volume shell_volume33783 ų
Envelope diameter envelope_diameter117.9
Shell Rg shell_rg35.36
Envelope Rg envelope_rg30.25
Shape Rg shape_rg29.91
Total Rg total_rg30.49
Total atoms total_atoms5584
Residues n_residues680
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 dmax111.5
Rg (real space) rg_real30.69
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real9.6810e+07
I(0) uncertainty (real space) i0_real_error1.6450e+06
Rg (reciprocal space) rg_reciprocal30.57
I(0) (reciprocal space) i0_reciprocal96800000.0000
Solution quality estimate total_estimate0.7990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.0
Skewness Skewness skewness0.628
Kurtosis Kurtosis kurtosis0.019
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha42340000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.601; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.653; Smooth: 0.927

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_idd1an9a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.4 — Nucleotide-binding domain
Superfamily Superfamily superfamilyc.4.1 — Nucleotide-binding domain
Family Family familyc.4.1.2 — D-aminoacid oxidase, N-terminal domain
Domain ID domain_idd1an9a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamilyd.16.1 — FAD-linked reductases, C-terminal domain
Family Family familyd.16.1.3 — D-aminoacid oxidase-like
Domain ID domain_idd1an9b1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.4 — Nucleotide-binding domain
Superfamily Superfamily superfamilyc.4.1 — Nucleotide-binding domain
Family Family familyc.4.1.2 — D-aminoacid oxidase, N-terminal domain
Domain ID domain_idd1an9b2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamilyd.16.1 — FAD-linked reductases, C-terminal domain
Family Family familyd.16.1.3 — D-aminoacid oxidase-like

CATH v4.4 (4 domains)

Domain ID domain_id1an9A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id1an9A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology9 — D-Amino Acid Oxidase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — D-Amino Acid Oxidase, subunit A, domain 2
Domain ID domain_id1an9B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id1an9B02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology9 — D-Amino Acid Oxidase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — D-Amino Acid Oxidase, subunit A, domain 2

8. Citations (2)

9. Files and Curves (10)