9uyy

Crystal structure of the indoleamine 2,3-dioxygenagse 2 (IDO2) complexed with L-Trp

Method: X-RAY DIFFRACTION Dmax: 105.7 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Indoleamine 2,3-dioxygenase 2

Homo sapiens

UniProt P0AEY0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–392 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 5 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 TRP TRYPTOPHAN × 1 CYN CYANIDE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;PEG 3350, Sodium citrate tribasic dihydrate Resolution 2.25 Å R-free 0.300

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.

109 other PDB entries and 148 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 19–384; UniProt 27–392

Maltose/maltodextrin-binding periplasmic protein,Indoleamine 2,3-dioxygenase 2

Homo sapiens

UniProt Q6ZQW0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 10–407 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 5 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 TRP TRYPTOPHAN × 1 CYN CYANIDE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;277 K;PEG 3350, Sodium citrate tribasic dihydrate Resolution 2.25 Å R-free 0.300

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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name I23O2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 385–782; UniProt 10–407

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 9uyy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9uyy
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9uyy
Deposition date deposition_date2025-05-16
最后修订 last_revision2026-04-08
Structure title titleCrystal structure of the indoleamine 2,3-dioxygenagse 2 (IDO2) complexed with L-Trp
Keywords keywordsHEM protein, Complex, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.51
Radius of gyration Rg (electron density) rg_electron32.20
Forward intensity I(0) i0103836000.00
Molecular weight molecular_weight84301.0 kDa
Excluded volume excluded_volume106670 ų
Envelope volume envelope_volume129580 ų
Hydration-shell volume shell_volume34433 ų
Envelope diameter envelope_diameter109.9
Shell Rg shell_rg38.14
Envelope Rg envelope_rg32.06
Shape Rg shape_rg32.18
Total Rg total_rg32.75
Total atoms total_atoms5951
Residues n_residues747
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 dmax105.7
Rg (real space) rg_real32.69
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.0380e+08
I(0) uncertainty (real space) i0_real_error1.5540e+06
Rg (reciprocal space) rg_reciprocal32.62
I(0) (reciprocal space) i0_reciprocal103800000.0000
Solution quality estimate total_estimate0.8691
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.2
Skewness Skewness skewness0.395
Kurtosis Kurtosis kurtosis-0.608
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46540000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.853; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.899; Smooth: 0.836

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)