1lp1

Protein Z in complex with an in vitro selected affibody

Method: X-RAY DIFFRACTION Dmax: 52.6 Å Quality: GOOD

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

Immunoglobulin G binding protein A

Staphylococcus aureus

UniProt P38507

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 212–269 Fragment:RESIDUES 2-58 Mutation:A1V, G29A Affibody binding protein Z × 1 SO4 SULFATE ION × 4 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;MgSO4, MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.30 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 212–269 Fragment:RESIDUES 2-58 Mutation:A1V, G29A Affibody binding protein Z × 2 SO4 SULFATE ION × 8 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;MgSO4, MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.30 Å R-free 0.256

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.

66 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPA2_STAAU
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–58; UniProt 212–269

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 1lp1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lp1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lp1
Deposition date deposition_date2002-05-07
Structure title titleProtein Z in complex with an in vitro selected affibody
Keywords keywordsin vitro evolved, protein-protein complex, three-helix bundle, affibody, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.22
Radius of gyration Rg (electron density) rg_electron14.03
Forward intensity I(0) i03522550.00
Molecular weight molecular_weight12685.0 kDa
Excluded volume excluded_volume15630 ų
Envelope volume envelope_volume17579 ų
Hydration-shell volume shell_volume11035 ų
Envelope diameter envelope_diameter51.5
Shell Rg shell_rg19.27
Envelope Rg envelope_rg14.57
Shape Rg shape_rg13.98
Total Rg total_rg15.20
Total atoms total_atoms889
Residues n_residues109
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 dmax52.6
Rg (real space) rg_real15.17
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real3.5230e+06
I(0) uncertainty (real space) i0_real_error3.9710e+04
Rg (reciprocal space) rg_reciprocal15.17
I(0) (reciprocal space) i0_reciprocal3523000.0000
Solution quality estimate total_estimate0.7846
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.9
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.203
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha443100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.743; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1lp1a_
Class classa — All alpha proteins
Fold Fold folda.8 — immunoglobulin/albumin-binding domain-like
Superfamily Superfamily superfamilya.8.1 — Bacterial immunoglobulin/albumin-binding domains
Family Family familya.8.1.1 — Immunoglobulin-binding protein A modules
Domain ID domain_idd1lp1b_
Class classa — All alpha proteins
Fold Fold folda.8 — immunoglobulin/albumin-binding domain-like
Superfamily Superfamily superfamilya.8.1 — Bacterial immunoglobulin/albumin-binding domains
Family Family familya.8.1.1 — Immunoglobulin-binding protein A modules

CATH v4.4 (2 domains)

Domain ID domain_id1lp1A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C
Domain ID domain_id1lp1B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily420 — Immunoglobulin FC, subunit C

8. Citations (1)

9. Files and Curves (10)