SAXSdb — 4b60

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

FIBRONECTIN-BINDING PROTEIN A

STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	FIBRINOGEN GAMMA CHAIN × 1 （P02679） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	FIBRINOGEN GAMMA CHAIN × 1 （P02679） CALCIUM ION × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	FIBRONECTIN-BINDING PROTEIN A × 1 （P14738） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	FIBRONECTIN-BINDING PROTEIN A × 1 （P14738） CALCIUM ION × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4b60
Deposition date deposition_date	2012-08-08
Structure title title	Structure of rFnBPA(189-505) in complex with fibrinogen gamma chain C- terminal peptide
Keywords keywords	CELL ADHESION, FNBPA, FIBRINOGEN, FIBRINOGEN BINDING; CELL ADHESION
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

4b60__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

4b60__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4b60__assembly_2__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	23.37 Å
Rg (electron density)	22.68 Å
Total Rg	23.53 Å
Atom count	2371
Residues	305
Excluded volume	41627 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4b60__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`4b60__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	FIBRONECTIN-BINDING PROTEIN A
Molecular weight formula_weight	35755.3 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	5204

GPAMAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKA

Source Source

Source organism organism	STAPHYLOCOCCUS AUREUS SUBSP. AUREUS NCTC 8325
NCBI taxonomy ID ncbi_taxonomy_id	93061
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	FIBRINOGEN GAMMA CHAIN
Molecular weight formula_weight	1691.8 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

GEGQQHHLGGAKQAGDV

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	406

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id	4b60A01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1280 —

Domain ID domain_id	4b60A02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1290 —

Domain ID domain_id	4b60B01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1280 —

Domain ID domain_id	4b60B02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	1290 —

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Unit-cell length a length_a	37.510 Å
Unit-cell length b length_b	59.050 Å
Unit-cell length c length_c	73.490 Å
Unit-cell angle α angle_alpha	91.86 °
Unit-cell angle β angle_beta	98.05 °
Unit-cell angle γ angle_gamma	97.87 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	1.830 Å
Low-resolution limit resolution_low	58.410 Å
R factor r_factor	0.2009
R_work r_work	0.1985
R_free r_free	0.2459

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

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

FIBRONECTIN-BINDING PROTEIN A

State in the Current Structure

Other States of the Same Protein in the Database

FIBRINOGEN GAMMA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4b60__assembly_2__model_1

4b60__assembly_2__model_1 | I(q)

4b60__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)

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

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

FIBRONECTIN-BINDING PROTEIN A

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

FIBRINOGEN GAMMA CHAIN

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4b60__assembly_2__model_1

4b60__assembly_2__model_1 | I(q)

4b60__assembly_2__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

7. Citations (1)