SAXSdb — 1h0t

▼

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

IMMUNOGLOBULIN G BINDING PROTEIN A

STAPHYLOCOCCUS AUREUS

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	Fragment：RESIDUES 213-269	ZSPA-1 AFFIBODY × 1	SOLUTION NMR NMR measurement conditions：pH 5.6；303 K；Pressure 1	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.

Other PDB	Difference from Current Entry 1H0T	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DEE Structure of S. aureus protein A bound to a human IgM Fab Deposited 1999-11-15	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain G 100–153（54 aa） Fragment：RECOMBINANT DOMAIN D	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；MPEG 5000, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.70 Å R-free 0.281
1DEE Structure of S. aureus protein A bound to a human IgM Fab Deposited 1999-11-15	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain H 100–153（54 aa） Fragment：RECOMBINANT DOMAIN D	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；MPEG 5000, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K	Resolution 2.70 Å R-free 0.281
1FC2 Crystallographic Refinement and Atomic Models of a Human FC Fragment and its Complex with Fragment B of Protein A from Staphylococcus Aureus at 2.9-and 2.8-Angstroms Resolution Deposited 1981-05-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 212–269（58 aa）	Not recorded	SO4 SULFATE ION × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
4Y4Y T=1 capsid structure of SeMV Ndel65CP fused with B-domain of S. aureus protein SpA at the N-terminus (C2 crystal form) Deposited 2015-02-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain A 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain B 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain C 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain D 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain E 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain F 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain G 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain H 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain I 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain J 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain K 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain L 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain M 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain N 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain O 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain P 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain Q 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain R 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain S 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain T 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain U 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain V 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain W 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain X 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain Y 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain Z 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain a 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain b 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain c 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268 Chain d 158–211（54 aa） Fragment：UNP RESIDUES 158-211, RESIDUES 66-268	Not recorded	SO4 SULFATE ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；15-20% PEG 4000, 5% Iso-propanol, 100 mM Sodium citrate	Resolution 3.00 Å R-free 0.200
4Y5Z T=1 capsid structure of SeMV Ndel65CP fused with B-domain of S. aureus protein SpA at the N-terminus (P1 crystal form) Deposited 2015-02-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 60 PDB declaration: 60-meric	Chain 0 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain 1 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain 2 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain 3 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain 4 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain 5 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain 6 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain 7 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain A 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain B 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain C 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain D 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain E 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain F 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain G 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain H 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain I 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain J 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain K 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain L 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain M 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain N 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain O 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain P 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain Q 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain R 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain S 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain T 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain U 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain V 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain W 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain X 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain Y 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain Z 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain a 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain b 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain c 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain d 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain e 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain f 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain g 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain h 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain i 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain j 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain k 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain l 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain m 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain n 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain o 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain p 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain q 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain r 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain s 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain t 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain u 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain v 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain w 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain x 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain y 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268 Chain z 158–211（54 aa） Fragment：UNP RESIDUES 158-211,UNP RESIDUES 66-268	Not recorded	SO4 SULFATE ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；295 K；15-25% PEG 400, 0.2M magnesium chloride, 0.1M HEPES	Resolution 2.95 Å R-free 0.249
9BDE Middle Region of Apolipoprotein B 100 bound to Low Density Lipoprotein Receptor Deposited 2024-04-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 278–327（50 aa） Fragment：;residues 27-384 (Uniprot numbering),residues 278-327 (Uniprot numbering),103-151 (Uniprot numbering),residues 440-497 (Uniprot numbering) ; Chain B 103–151（49 aa） Fragment：;residues 27-384 (Uniprot numbering),residues 278-327 (Uniprot numbering),103-151 (Uniprot numbering),residues 440-497 (Uniprot numbering) ;	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CA CALCIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.18 Å
9HXS CS-ROSETTA Structure of the Z Domain of the IgG-Binding Staphylococcal Protein A Deposited 2025-01-08	Different construct Different oligomeric state Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 212–269（58 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 150；Pressure 1 NMR sample composition 2 mg/mL [U-100% 13C; U-100% 15N] Protein Z, 25 mM MES, 1 mM CaCl2, 93% H2O/7% D2O \| 93% H2O/7% D2O	Resolution not provided
9M5D Crystal structure of S. aureus protein A bound to a human single-domain antibody Deposited 2025-03-05	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 93–153（61 aa） Chain H 93–153（61 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；25% w/v Polyethylene glycol 3350, 0.2M Magnesium chloride and 0.1M BIS-Tris 5.5	Resolution 3.57 Å R-free 0.271
9M6J Crystal structure of S. aureus protein A bound to a camelid single-domain antibody Deposited 2025-03-07	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 93–153（61 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；2.0 M Ammonium sulfate	Resolution 2.00 Å R-free 0.226
9M6O Crystal structure of S. aureus protein A bound to a camelid single-domain antibody Deposited 2025-03-07	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 93–153（61 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；25% w/v Polyethylene glycol 3350 and 0.1M Citric acid 3.5	Resolution 1.49 Å R-free 0.257
9M6O Crystal structure of S. aureus protein A bound to a camelid single-domain antibody Deposited 2025-03-07	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 93–153（61 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；25% w/v Polyethylene glycol 3350 and 0.1M Citric acid 3.5	Resolution 1.49 Å R-free 0.257
9QBJ Legobody dimer Deposited 2025-03-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 8 PDB declaration: octameric	Chain I 295–321（27 aa） Chain J 295–321（27 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SPA1_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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1h0t
Deposition date deposition_date	2002-06-27
Structure title title	An affibody in complex with a target protein: structure and coupled folding
Keywords keywords	;IMMUNE SYSTEM, PROTEIN-PROTEIN INTERACTIONS, PROTEIN ENGINEERING, MOLECULAR RECOGNITION, NMR SPECTROSCOPY, MOLTEN GLOBULE, INDUCED FIT, COUPLED PROTEIN FOLDING, AFFIBODY, IGG BINDING PROTEIN A ;; IMMUNE SYSTEM
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	13.97 Å
Radius of gyration Rg (electron density) rg_electron	13.81 Å
Forward intensity I(0) i0	3817810000.00
Molecular weight molecular_weight	523110.0 kDa
Excluded volume excluded_volume	653170 Å³
Envelope volume envelope_volume	28732 Å³
Hydration-shell volume shell_volume	14797 Å³
Envelope diameter envelope_diameter	55.1 Å
Shell Rg shell_rg	22.45 Å
Envelope Rg envelope_rg	17.19 Å
Shape Rg shape_rg	13.77 Å
Total Rg total_rg	14.01 Å
Total atoms total_atoms	73640
Residues n_residues	4640
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	44.0 Å
Rg (real space) rg_real	13.93 Å
Rg uncertainty (real space) rg_real_error	0.13 Å
I(0) (real space) i0_real	3.8170e+09
I(0) uncertainty (real space) i0_real_error	3.2840e+07
Rg (reciprocal space) rg_reciprocal	13.93 Å
I(0) (reciprocal space) i0_reciprocal	3818000000.0000
Solution quality estimate total_estimate	0.6785
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	42.9 Å
Skewness Skewness skewness	0.217
Kurtosis Kurtosis kurtosis	-0.450
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0806
Highest regularization parameter α highest_alpha	212200.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.999

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	IMMUNOGLOBULIN G BINDING PROTEIN A
Molecular weight formula_weight	6648.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	73640

VDNKFNKEQQNAFYEILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEAKKLNDAQAPK

来源 Source

来源生物 organism	STAPHYLOCOCCUS AUREUS
NCBI Class编号 ncbi_taxonomy_id	1280
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	ZSPA-1 AFFIBODY
Molecular weight formula_weight	6447.3 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

VDNKFNKELSVAGREIVTLPNLNDPQKKAFIFSLWDDPSQSANLLAEAKKLNDAQAPK

来源 Source

来源生物 organism	SYNTHETIC CONSTRUCT
NCBI Class编号 ncbi_taxonomy_id	32630
宿主生物 host_organism	ESCHERICHIA COLI

▼

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1h0ta1
Class class	a — All alpha proteins
Fold Fold fold	a.8 — immunoglobulin/albumin-binding domain-like
Superfamily Superfamily superfamily	a.8.1 — Bacterial immunoglobulin/albumin-binding domains
Family Family family	a.8.1.1 — Immunoglobulin-binding protein A modules

Domain ID domain_id	d1h0ta2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d1h0tb_
Class class	a — All alpha proteins
Fold Fold fold	a.8 — immunoglobulin/albumin-binding domain-like
Superfamily Superfamily superfamily	a.8.1 — Bacterial immunoglobulin/albumin-binding domains
Family Family family	a.8.1.1 — Immunoglobulin-binding protein A modules

CATH v4.4 (2 domains)

Domain ID domain_id	1h0tA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

Domain ID domain_id	1h0tB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	420 — Immunoglobulin FC, subunit C

▶

8. Citations (1)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

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

fit	/app/data/saxs_computation/h0/1h0t/1h0t.fit
pddf	/app/data/pr_computation/h0/1h0t/1h0t.pr.out
profile	/app/data/saxs_computation/h0/1h0t/1h0t.dat

An affibody in complex with a target protein: structure and coupled folding

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

IMMUNOGLOBULIN G BINDING PROTEIN A

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)