7v5t

Crystal structure of human bleomycin hydrolase C73S mutant

Method: X-RAY DIFFRACTION Dmax: 87.3 Å Quality: GOOD

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

Bleomycin hydrolase

Homo sapiens

UniProt Q13867

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–455 Mutation:C73S No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;30% (w/v) PEG 400, 0.1mM CHES, pH 9.5 Resolution 3.25 Å R-free 0.193

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.

5 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BLMH_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–475; UniProt 1–455

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 7v5t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v5t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v5t
Deposition date deposition_date2021-08-18
Structure title titleCrystal structure of human bleomycin hydrolase C73S mutant
Keywords keywordscysteine protease, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.35
Radius of gyration Rg (electron density) rg_electron24.42
Forward intensity I(0) i045511900.00
Molecular weight molecular_weight52537.0 kDa
Excluded volume excluded_volume65755 ų
Envelope volume envelope_volume83554 ų
Hydration-shell volume shell_volume28367 ų
Envelope diameter envelope_diameter90.5
Shell Rg shell_rg31.73
Envelope Rg envelope_rg25.52
Shape Rg shape_rg24.39
Total Rg total_rg25.31
Total atoms total_atoms3693
Residues n_residues455
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 dmax87.3
Rg (real space) rg_real25.35
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real4.5510e+07
I(0) uncertainty (real space) i0_real_error5.8930e+05
Rg (reciprocal space) rg_reciprocal25.35
I(0) (reciprocal space) i0_reciprocal45510000.0000
Solution quality estimate total_estimate0.8686
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.1
Skewness Skewness skewness0.393
Kurtosis Kurtosis kurtosis-0.187
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7635000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)