4b60

Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide

Method: X-RAY DIFFRACTION Dmax: 95.0 Å Quality: REASONABLE

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

FIBRONECTIN-BINDING PROTEIN A

STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325

UniProt P14738

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 189–505 Fragment:N2N3, RESIDUES 189-505 FIBRINOGEN GAMMA CHAIN × 1 (P02679) X-RAY DIFFRACTION X-ray crystallization conditions:PEG 2K MME 25%, 0.2 M CA AC, ISOPROPANOL 10% Resolution 1.83 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 189–505 Fragment:N2N3, RESIDUES 189-505 FIBRINOGEN GAMMA CHAIN × 1 (P02679) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:PEG 2K MME 25%, 0.2 M CA AC, ISOPROPANOL 10% Resolution 1.83 Å R-free 0.246

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.

5 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FNBA_STAA8
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–321; UniProt 189–505 Author chain B; PDBConstruct 5–321; UniProt 189–505

FIBRINOGEN GAMMA CHAIN

OrganismNot specified

UniProt P02679

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 C; UniProt 421–437 Fragment:C-TERMINUS, RESIDUES 421-433 FIBRONECTIN-BINDING PROTEIN A × 1 (P14738) X-RAY DIFFRACTION X-ray crystallization conditions:PEG 2K MME 25%, 0.2 M CA AC, ISOPROPANOL 10% Resolution 1.83 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 421–437 Fragment:C-TERMINUS, RESIDUES 421-433 FIBRONECTIN-BINDING PROTEIN A × 1 (P14738) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:PEG 2K MME 25%, 0.2 M CA AC, ISOPROPANOL 10% Resolution 1.83 Å R-free 0.246

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.

36 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–17; UniProt 421–437 Author chain D; PDBConstruct 1–17; UniProt 421–437

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 4b60

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4b60
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4b60
Deposition date deposition_date2012-08-08
Structure title titleStructure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide
Keywords keywordsCELL ADHESION, FNBPA, FIBRINOGEN, FIBRINOGEN BINDING; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.46
Radius of gyration Rg (electron density) rg_electron28.64
Forward intensity I(0) i080109600.00
Molecular weight molecular_weight67947.0 kDa
Excluded volume excluded_volume84001 ų
Envelope volume envelope_volume107570 ų
Hydration-shell volume shell_volume32014 ų
Envelope diameter envelope_diameter97.8
Shell Rg shell_rg35.17
Envelope Rg envelope_rg28.38
Shape Rg shape_rg28.62
Total Rg total_rg29.31
Total atoms total_atoms4792
Residues n_residues619
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 dmax95.0
Rg (real space) rg_real29.47
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real8.0110e+07
I(0) uncertainty (real space) i0_real_error1.2470e+06
Rg (reciprocal space) rg_reciprocal29.47
I(0) (reciprocal space) i0_reciprocal80110000.0000
Solution quality estimate total_estimate0.6806
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.2
Skewness Skewness skewness0.350
Kurtosis Kurtosis kurtosis-0.313
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14460000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 0.092; Positv: 1.000; Valcen: 0.996; Smooth: 0.809

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id4b60A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1280
Domain ID domain_id4b60A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1290
Domain ID domain_id4b60B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1280
Domain ID domain_id4b60B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily1290

8. Citations (1)

9. Files and Curves (10)