1byl

BLEOMYCIN RESISTANCE PROTEIN FROM STREPTOALLOTEICHUS HINDUSTANUS

Method: X-RAY DIFFRACTION Dmax: 58.8 Å Quality: REASONABLE

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

PROTEIN (BLEOMYCIN RESISTANCE PROTEIN)

Streptoalloteichus hindustanus

UniProt P17493

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 1–124 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;SEE REFERENCE 2, pH 6.0 Resolution 2.30 Å

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BLE_STRHI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–125; UniProt 1–124

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 1byl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1byl
Deposition date deposition_date1998-10-17
Structure title titleBLEOMYCIN RESISTANCE PROTEIN FROM STREPTOALLOTEICHUS HINDUSTANUS
Keywords keywordsANTIBIOTIC RESISTANCE, BLEOMYCIN, DRUG SEQUESTERING, CHAIN SWAPPING, ANTIBIOTIC; ANTIBIOTIC
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.11
Radius of gyration Rg (electron density) rg_electron14.90
Forward intensity I(0) i03750930.00
Molecular weight molecular_weight13542.0 kDa
Excluded volume excluded_volume16875 ų
Envelope volume envelope_volume20149 ų
Hydration-shell volume shell_volume11935 ų
Envelope diameter envelope_diameter60.0
Shell Rg shell_rg20.31
Envelope Rg envelope_rg15.73
Shape Rg shape_rg14.85
Total Rg total_rg16.19
Total atoms total_atoms959
Residues n_residues122
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 dmax58.8
Rg (real space) rg_real16.09
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real3.7510e+06
I(0) uncertainty (real space) i0_real_error4.9160e+04
Rg (reciprocal space) rg_reciprocal16.09
I(0) (reciprocal space) i0_reciprocal3751000.0000
Solution quality estimate total_estimate0.7476
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.1
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis0.141
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha609500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.594; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.933; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1byla_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.32 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Superfamily Superfamily superfamilyd.32.1 — Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase
Family Family familyd.32.1.2 — Antibiotic resistance proteins

CATH v4.4 (1 domains)

Domain ID domain_id1bylA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology180 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase; domain 1
Homologous superfamily homologous superfamily10 — 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

8. Citations (4)

9. Files and Curves (10)