1hy2

MINIPROTEIN MP-1 COMPLEX WITH STREPTAVIDIN

Method: X-RAY DIFFRACTION Dmax: 68.6 Å Quality: EXCELLENT

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

STREPTAVIDIN

Streptomyces avidinii

UniProt P22629

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 heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–129 Chain B; UniProt 1–129 Chain C; UniProt 1–129 Chain D; UniProt 1–129 Not recorded MP-1 × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4;298 K;100mM potassium acetate, ammonium sulfate, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.258

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.

312 other PDB entries and 368 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAV_STRAV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–129; UniProt 1–129 Author chain B; PDBConstruct 1–129; UniProt 1–129 Author chain C; PDBConstruct 1–129; UniProt 1–129 Author chain D; PDBConstruct 1–129; UniProt 1–129

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 1hy2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1hy2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1hy2
Deposition date deposition_date2001-01-17
Structure title titleMINIPROTEIN MP-1 COMPLEX WITH STREPTAVIDIN
Keywords keywordsCONFORMATIONAL ENSEMBLE, MINI-PROTEINS, DISULPHIDE CONSTRAINED LOOPS, ENTROPICALLY RESTRAINED PROTEINS, PEPTIDES, UNKNOWN FUNCTION; UNKNOWN FUNCTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.47
Radius of gyration Rg (electron density) rg_electron22.39
Forward intensity I(0) i058937200.00
Molecular weight molecular_weight56718.0 kDa
Excluded volume excluded_volume69512 ų
Envelope volume envelope_volume83312 ų
Hydration-shell volume shell_volume29653 ų
Envelope diameter envelope_diameter69.4
Shell Rg shell_rg30.23
Envelope Rg envelope_rg22.56
Shape Rg shape_rg22.35
Total Rg total_rg23.34
Total atoms total_atoms4000
Residues n_residues540
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 dmax68.6
Rg (real space) rg_real23.28
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real5.8940e+07
I(0) uncertainty (real space) i0_real_error6.8800e+05
Rg (reciprocal space) rg_reciprocal23.33
I(0) (reciprocal space) i0_reciprocal58940000.0000
Solution quality estimate total_estimate0.9110
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.7
Skewness Skewness skewness0.055
Kurtosis Kurtosis kurtosis-0.558
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16360000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.957; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1hy2a_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd1hy2b_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd1hy2c_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd1hy2d_
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin

CATH v4.4 (4 domains)

Domain ID domain_id1hy2A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1hy2B00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1hy2C00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1hy2D00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like

8. Citations (1)

9. Files and Curves (10)