2m5a

Protein A binding by an engineered Affibody molecule

Method: SOLUTION NMR Dmax: 51.9 Å Quality: REASONABLE

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 A; UniProt 213–269 Not recorded ZpA963 × 1 SOLUTION NMR NMR measurement conditions:pH 5.6;298 K;Ionic strength (raw mmCIF value) 0.095;Pressure ambient NMR sample composition:0.5 to 1 mM [U-99% 13C; U-99% 15N] Z domain, 25% molar excess mM ZpA963, 93% H2O/7% D2O | 93% H2O/7% D2O NMR sample composition:0.5 to 1.0 mM [U-99% 13C; U-99% 15N] ZpA963, 25 5 molar excess mM Z domain, 93% H2O/7% D2O | 93% H2O/7% D2O Resolution not provided

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 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPA_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–58; UniProt 213–269

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 2m5a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2m5a
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2m5a
Deposition date deposition_date2013-02-19
Structure title titleProtein A binding by an engineered Affibody molecule
Keywords keywordsbinding protein, protein engineering, protein A, Z domain, Affibody molecule, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.14
Radius of gyration Rg (electron density) rg_electron13.90
Forward intensity I(0) i0986136000.00
Molecular weight molecular_weight260490.0 kDa
Excluded volume excluded_volume323600 ų
Envelope volume envelope_volume25336 ų
Hydration-shell volume shell_volume13922 ų
Envelope diameter envelope_diameter64.9
Shell Rg shell_rg21.40
Envelope Rg envelope_rg16.22
Shape Rg shape_rg13.84
Total Rg total_rg14.22
Total atoms total_atoms36460
Residues n_residues2320
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 dmax51.9
Rg (real space) rg_real14.09
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real9.8610e+08
I(0) uncertainty (real space) i0_real_error1.1340e+07
Rg (reciprocal space) rg_reciprocal14.10
I(0) (reciprocal space) i0_reciprocal986100000.0000
Solution quality estimate total_estimate0.5694
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.277
Kurtosis Kurtosis kurtosis0.057
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha277300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.563; Stabil: 0.998; Sysdev: 0.256; Positv: 1.000; Valcen: 0.946; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2m5aa1
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_idd2m5aa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2m5ab_
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_id2m5aA00
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_id2m5aB00
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)