4cpi

streptavidin A86D mutant with love-hate ligand 4

Method: X-RAY DIFFRACTION Dmax: 96.2 Å Quality: GOOD

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 37–163 Chain D; UniProt 37–163 Fragment:RESIDUES 37-163 Mutation:YES LH4 5-[(3aS,4S,6aR)-2-oxo-hexahydro-1H-thieno[3,4- d]imidazolidin-4-yl]-N'-{2,6-bis[4-(morpholine-4- sulfonyl)phenyl]phenyl}pentanehydrazide × 4 PEG DI(HYDROXYETHYL)ETHER × 4 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;CONDITION A9 OF THE MORPHEUS SCREEN: 0.1 M BICINE/TRIZMA BASE PH 8.5, 10% W/V POLYETHYLENE GLYCOL 20,000, 20% V/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 550, 30 MM MAGNESIUM CHLORIDE AND 30 MM CALCIUM CHLORIDE. SITTING DROP. Resolution 1.54 Å R-free 0.181
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 37–163 Chain B; UniProt 37–163 Fragment:RESIDUES 37-163 Mutation:YES LH4 5-[(3aS,4S,6aR)-2-oxo-hexahydro-1H-thieno[3,4- d]imidazolidin-4-yl]-N'-{2,6-bis[4-(morpholine-4- sulfonyl)phenyl]phenyl}pentanehydrazide × 4 PEG DI(HYDROXYETHYL)ETHER × 4 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;CONDITION A9 OF THE MORPHEUS SCREEN: 0.1 M BICINE/TRIZMA BASE PH 8.5, 10% W/V POLYETHYLENE GLYCOL 20,000, 20% V/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 550, 30 MM MAGNESIUM CHLORIDE AND 30 MM CALCIUM CHLORIDE. SITTING DROP. Resolution 1.54 Å R-free 0.181
3 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 37–163 Chain D; UniProt 37–163 Fragment:RESIDUES 37-163 Mutation:YES LH4 5-[(3aS,4S,6aR)-2-oxo-hexahydro-1H-thieno[3,4- d]imidazolidin-4-yl]-N'-{2,6-bis[4-(morpholine-4- sulfonyl)phenyl]phenyl}pentanehydrazide × 4 PEG DI(HYDROXYETHYL)ETHER × 4 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;CONDITION A9 OF THE MORPHEUS SCREEN: 0.1 M BICINE/TRIZMA BASE PH 8.5, 10% W/V POLYETHYLENE GLYCOL 20,000, 20% V/V POLYETHYLENE GLYCOL MONOMETHYL ETHER 550, 30 MM MAGNESIUM CHLORIDE AND 30 MM CALCIUM CHLORIDE. SITTING DROP. Resolution 1.54 Å R-free 0.181

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 366 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 1–127; UniProt 37–163 Author chain B; PDBConstruct 1–127; UniProt 37–163 Author chain C; PDBConstruct 1–127; UniProt 37–163 Author chain D; PDBConstruct 1–127; UniProt 37–163

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 4cpi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cpi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4cpi
Deposition date deposition_date2014-02-06
Structure title titlestreptavidin A86D mutant with love-hate ligand 4
Keywords keywordsBIOTIN BINDING PROTEIN, AVIDIN, BIOTIN, STRAIN, BIOTINYLATED, STERIC CLASH, STRAINED, HINDERED, FORCE, LIGAND SERIES, AFFINITY; BIOTIN BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.82
Radius of gyration Rg (electron density) rg_electron30.22
Forward intensity I(0) i048865000.00
Molecular weight molecular_weight52922.0 kDa
Excluded volume excluded_volume65239 ų
Envelope volume envelope_volume87717 ų
Hydration-shell volume shell_volume24815 ų
Envelope diameter envelope_diameter102.4
Shell Rg shell_rg36.41
Envelope Rg envelope_rg29.77
Shape Rg shape_rg30.21
Total Rg total_rg30.81
Total atoms total_atoms3738
Residues n_residues474
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 dmax96.2
Rg (real space) rg_real30.93
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real4.8860e+07
I(0) uncertainty (real space) i0_real_error7.0710e+05
Rg (reciprocal space) rg_reciprocal30.89
I(0) (reciprocal space) i0_reciprocal48860000.0000
Solution quality estimate total_estimate0.8739
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.5
Skewness Skewness skewness0.267
Kurtosis Kurtosis kurtosis-0.786
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6142000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.793; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4cpia_
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_idd4cpib_
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_idd4cpic_
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_idd4cpid_
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_id4cpiA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id4cpiB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id4cpiC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id4cpiD00
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)