1bwd

INOSAMINE-PHOSPHATE AMIDINOTRANSFERASE STRB1 FROM STREPTOMYCES GRISEUS

Method: X-RAY DIFFRACTION Dmax: 111.2 Å Quality: REASONABLE

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

PROTEIN (INOSAMINE-PHOSPHATE AMIDINOTRANSFERASE)

Streptomyces griseus

UniProt P08078

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 1–347 Chain B; UniProt 1–347 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5;20% PEG 4000, 0.1 M SODIUM CITRAT BUFFER (PH 5.0), 0.2 M AMMONIUM ACETATE Resolution 3.10 Å R-free 0.265

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name STRB1_STRGR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–348; UniProt 1–347 Author chain B; PDBConstruct 1–348; UniProt 1–347

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 1bwd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bwd
Deposition date deposition_date1998-09-23
Structure title titleINOSAMINE-PHOSPHATE AMIDINOTRANSFERASE STRB1 FROM STREPTOMYCES GRISEUS
Keywords keywordsAMIDINOTRANSFERASE, STREPTOMYCIN, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.33
Radius of gyration Rg (electron density) rg_electron35.10
Forward intensity I(0) i093334600.00
Molecular weight molecular_weight77342.0 kDa
Excluded volume excluded_volume96571 ų
Envelope volume envelope_volume124080 ų
Hydration-shell volume shell_volume29436 ų
Envelope diameter envelope_diameter113.8
Shell Rg shell_rg41.55
Envelope Rg envelope_rg34.46
Shape Rg shape_rg35.10
Total Rg total_rg35.53
Total atoms total_atoms5455
Residues n_residues696
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 dmax111.2
Rg (real space) rg_real35.58
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real9.3330e+07
I(0) uncertainty (real space) i0_real_error1.6550e+06
Rg (reciprocal space) rg_reciprocal35.43
I(0) (reciprocal space) i0_reciprocal93320000.0000
Solution quality estimate total_estimate0.7351
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.333
Kurtosis Kurtosis kurtosis-0.948
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57820000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.481; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.638; Smooth: 0.470

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1bwda_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.126 — Pentein, beta/alpha-propeller
Superfamily Superfamily superfamilyd.126.1 — Pentein
Family Family familyd.126.1.2 — Amidinotransferase
Domain ID domain_idd1bwdb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.126 — Pentein, beta/alpha-propeller
Superfamily Superfamily superfamilyd.126.1 — Pentein
Family Family familyd.126.1.2 — Amidinotransferase

CATH v4.4 (2 domains)

Domain ID domain_id1bwdA00
Class class3 — Alpha Beta
Architecture architecture75 — 5-stranded Propeller
Topology topology10 — L-arginine/glycine Amidinotransferase; Chain A
Homologous superfamily homologous superfamily10 — L-arginine/glycine Amidinotransferase; Chain A
Domain ID domain_id1bwdB00
Class class3 — Alpha Beta
Architecture architecture75 — 5-stranded Propeller
Topology topology10 — L-arginine/glycine Amidinotransferase; Chain A
Homologous superfamily homologous superfamily10 — L-arginine/glycine Amidinotransferase; Chain A

8. Citations (1)

9. Files and Curves (10)