6bpv

Crystal structure of cysteine-bound ferrous form of the matured F2-Tyr157 human cysteine dioxygenase

Method: X-RAY DIFFRACTION Dmax: 55.5 Å Quality: GOOD

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

Cysteine dioxygenase type 1

Homo sapiens

UniProt Q16878

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–200 Non-standard monomer:Yes (specific site not provided by mmCIF) FE2 FE (II) ION × 1 CYS CYSTEINE × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;0.1 M MES, 2 M ammonium sulfate, 2% PEG400 Resolution 1.95 Å R-free 0.179

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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDO1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–200; UniProt 2–200

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 6bpv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6bpv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6bpv
Deposition date deposition_date2017-11-26
Structure title titleCrystal structure of cysteine-bound ferrous form of the matured F2-Tyr157 human cysteine dioxygenase
Keywords keywordsCysteine, Cys-Tyr cofactor, iron, unnatural amino acid, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.45
Radius of gyration Rg (electron density) rg_electron16.35
Forward intensity I(0) i09754370.00
Molecular weight molecular_weight21861.0 kDa
Excluded volume excluded_volume26817 ų
Envelope volume envelope_volume31105 ų
Hydration-shell volume shell_volume15976 ų
Envelope diameter envelope_diameter56.2
Shell Rg shell_rg22.43
Envelope Rg envelope_rg16.72
Shape Rg shape_rg16.35
Total Rg total_rg17.33
Total atoms total_atoms1529
Residues n_residues186
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 dmax55.5
Rg (real space) rg_real17.36
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real9.7540e+06
I(0) uncertainty (real space) i0_real_error1.1530e+05
Rg (reciprocal space) rg_reciprocal17.37
I(0) (reciprocal space) i0_reciprocal9754000.0000
Solution quality estimate total_estimate0.8137
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.216
Kurtosis Kurtosis kurtosis-0.299
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2109000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.859; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6bpva_
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.1 — RmlC-like cupins
Family Family familyb.82.1.19 — Cysteine dioxygenase type I

CATH v4.4 (1 domains)

Domain ID domain_id6bpvA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls

8. Citations (1)

9. Files and Curves (10)