6bpt

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

Method: X-RAY DIFFRACTION Dmax: 63.0 Å Quality: REASONABLE

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 SO4 SULFATE ION × 4 GOL GLYCEROL × 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 2.40 Å R-free 0.202

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 6bpt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6bpt
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6bpt
Deposition date deposition_date2017-11-26
Structure title titleCrystal structure of ferrous form of the uncrosslinked 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_guinier17.43
Radius of gyration Rg (electron density) rg_electron16.35
Forward intensity I(0) i010064000.00
Molecular weight molecular_weight22214.0 kDa
Excluded volume excluded_volume27246 ų
Envelope volume envelope_volume31558 ų
Hydration-shell volume shell_volume16131 ų
Envelope diameter envelope_diameter59.2
Shell Rg shell_rg22.49
Envelope Rg envelope_rg16.79
Shape Rg shape_rg16.34
Total Rg total_rg17.35
Total atoms total_atoms1551
Residues n_residues185
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 dmax63.0
Rg (real space) rg_real17.34
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.0060e+07
I(0) uncertainty (real space) i0_real_error1.4340e+05
Rg (reciprocal space) rg_reciprocal17.35
I(0) (reciprocal space) i0_reciprocal10060000.0000
Solution quality estimate total_estimate0.5888
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.9
Skewness Skewness skewness0.231
Kurtosis Kurtosis kurtosis-0.271
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2819000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.559; Stabil: 0.973; Sysdev: 0.363; Positv: 1.000; Valcen: 0.967; 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_idd6bpta_
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_id6bptA00
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)