2a3x

Decameric crystal structure of human serum amyloid P-component bound to Bis-1,2-{[(Z)-2carboxy- 2-methyl-1,3-dioxane]- 5-yloxycarbonyl}-piperazine

Method: X-RAY DIFFRACTION D_max: 114.6 Å Quality: GOOD

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

Serum amyloid P-component

OrganismNot specified

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 homooligomer Homooligomer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain A； UniProt 20–223 Chain B； UniProt 20–223 Chain C； UniProt 20–223 Chain D； UniProt 20–223 Chain E； UniProt 20–223 Chain F； UniProt 20–223 Chain G； UniProt 20–223 Chain H； UniProt 20–223 Chain I； UniProt 20–223 Chain J； UniProt 20–223	Not recorded	CA CALCIUM ION × 20 CPK BIS-1,2-{[(Z)-2CARBOXY-2-METHYL-1,3-DIOXANE]-5-YLOXYCARBONYL}-PIPERAZINE × 3	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 5.5；294 K；sodium acetate, calcium acetate, PEG 8000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 3.00 Å R-free 0.282

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 2A3X	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1GYK Serum Amyloid P Component co-crystallised with MOBDG at neutral pH Deposited 2002-04-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	CA CALCIUM ION × 9 CDG METHYL 4,6-O-[(1R)-1-CARBOXYETHYLIDENE]-BETA-D-GALACTOPYRANOSIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；pH 8.00	Resolution 2.20 Å R-free 0.224
1LGN DECAMERIC DAMP COMPLEX OF HUMAN SERUM AMYLOID P COMPONENT Deposited 1996-12-04	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	CA CALCIUM ION × 10 D5M 2'-DEOXYADENOSINE-5'-MONOPHOSPHATE × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；277 K；3 + 3 UL HANGING DROPS AT 277K PROTEIN SOLUTION: 20 MG/ML PROTEIN, 10 MM TRIS-HCL, PH 8.0, 140 MM NACL, 20 MM DAMP, 0.02 % NA-AZIDE. RESERVOIR SOLUTION: 100 MM BIS-TRIS PROPANE- HCL PH 8.0, 20 MM CALCIUM CHLORIDE, 12-14 % (W/V) POLYETHYLENEGLYCOL 4000., vapor diffusion - hanging drop	Resolution 2.80 Å R-free 0.252
1SAC THE STRUCTURE OF PENTAMERIC HUMAN SERUM AMYLOID P COMPONENT Deposited 1994-01-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	CA CALCIUM ION × 10 ACY ACETIC ACID × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
2A3W Decameric structure of human serum amyloid P-component bound to Bis-1,2-{[(Z)-2-carboxy-2-methyl-1,3-dioxane]-5-yloxycarbamoyl}-ethane Deposited 2005-06-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa） Chain F 20–223（204 aa） Chain G 20–223（204 aa） Chain H 20–223（204 aa） Chain I 20–223（204 aa） Chain J 20–223（204 aa）	Not recorded	CA CALCIUM ION × 20 CPJ BIS-1,2-{[(Z)-2-CARBOXY-2-METHYL-1,3-DIOXANE]-5-YLOXYCARBAMOYL}-ETHANE × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；294 K；PEG 4000, PEG 400, sodium acetate, calcium acetate, sorbitol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.20 Å R-free 0.229
2A3W Decameric structure of human serum amyloid P-component bound to Bis-1,2-{[(Z)-2-carboxy-2-methyl-1,3-dioxane]-5-yloxycarbamoyl}-ethane Deposited 2005-06-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain K 20–223（204 aa） Chain L 20–223（204 aa） Chain M 20–223（204 aa） Chain N 20–223（204 aa） Chain O 20–223（204 aa） Chain P 20–223（204 aa） Chain Q 20–223（204 aa） Chain R 20–223（204 aa） Chain S 20–223（204 aa） Chain T 20–223（204 aa）	Not recorded	CA CALCIUM ION × 20 CPJ BIS-1,2-{[(Z)-2-CARBOXY-2-METHYL-1,3-DIOXANE]-5-YLOXYCARBAMOYL}-ETHANE × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；294 K；PEG 4000, PEG 400, sodium acetate, calcium acetate, sorbitol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.20 Å R-free 0.229
2A3Y Pentameric crystal structure of human serum amyloid P-component bound to Bis-1,2-{[(Z)-2carboxy-2-methyl-1,3-dioxane]-5-yloxycarbamoyl}-ethane. Deposited 2005-06-27	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	CA CALCIUM ION × 10 CPJ BIS-1,2-{[(Z)-2-CARBOXY-2-METHYL-1,3-DIOXANE]-5-YLOXYCARBAMOYL}-ETHANE × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；294 K；sodium actetate, calcium acetate, PEG 8000, PEG 400, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.00 Å R-free 0.250
2W08 The structure of serum amyloid P component bound to 0-phospho- threonine Deposited 2008-08-12	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	CA CALCIUM ION × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 TPO PHOSPHOTHREONINE × 5	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.06M TRIS-HCL PH8, 16% PEG 550MME, 0.01M CACL2, 0.08M NACL, 0.1% NAN3, 14.2MG/ML PROTEIN, 50MM LIGAND	Resolution 1.70 Å R-free 0.176
3D5O Structural recognition and functional activation of FcrR by innate pentraxins Deposited 2008-05-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	SO4 SULFATE ION × 16 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；2.0 M NH4SO4, 5% iso-propanol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.279
3KQR The structure of serum amyloid p component bound to phosphoethanolamine Deposited 2009-11-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	OPE PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER × 5 CA CALCIUM ION × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；0.06M TRIS-HCL pH8, 16% PEG 550MME, 0.01M CaCl2, 0.14M NaCl, 0.1% NaN3,14.2mg/ml Protein, 0.05M Ligand, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.50 Å R-free 0.161
4AVS Structure of N-Acetyl-L-Proline bound to Serum Amyloid P Component Deposited 2012-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CA CALCIUM ION × 10 N7P 1-ACETYL-L-PROLINE × 5	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；0.06 M TRIS-HCL, PH 8, 16% PEG 550 MME, 0.01 M CACL2, 0.08 M NACL AND 0.1% NAN3	Resolution 1.40 Å R-free 0.170
4AVT Structure of CPHPC bound to Serum Amyloid P Component Deposited 2012-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain C 20–223（204 aa） Chain E 20–223（204 aa） Chain G 20–223（204 aa） Chain I 20–223（204 aa）	Not recorded	CA CALCIUM ION × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 GHE (2R)-1-[6-[(2R)-2-carboxypyrrolidin-1-yl]-6-oxidanylidene-hexanoyl]pyrrolidine-2-carboxylic acid × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.6；60MM TRIS-HCL, 80MM NACL, 15% PEG550 MME, pH 7.6	Resolution 3.20 Å R-free 0.197
4AVT Structure of CPHPC bound to Serum Amyloid P Component Deposited 2012-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain B 20–223（204 aa） Chain D 20–223（204 aa） Chain F 20–223（204 aa） Chain H 20–223（204 aa） Chain J 20–223（204 aa）	Not recorded	CA CALCIUM ION × 10 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 GHE (2R)-1-[6-[(2R)-2-carboxypyrrolidin-1-yl]-6-oxidanylidene-hexanoyl]pyrrolidine-2-carboxylic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.6；60MM TRIS-HCL, 80MM NACL, 15% PEG550 MME, pH 7.6	Resolution 3.20 Å R-free 0.197
4AVV Structure of CPHPC bound to Serum Amyloid P Component Deposited 2012-05-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	ACT ACETATE ION × 8 GHE (2R)-1-[6-[(2R)-2-carboxypyrrolidin-1-yl]-6-oxidanylidene-hexanoyl]pyrrolidine-2-carboxylic acid × 5 CD CADMIUM ION × 35 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 SIA N-acetyl-alpha-neuraminic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 4.6；PH 4.6	Resolution 1.60 Å R-free 0.175
4AYU Structure of N-Acetyl-D-Proline bound to serum amyloid P component Deposited 2012-06-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain A 20–223（204 aa） Chain B 20–223（204 aa） Chain C 20–223（204 aa） Chain D 20–223（204 aa） Chain E 20–223（204 aa）	Not recorded	CA CALCIUM ION × 10 N8P N-ACETYL-D-PROLINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 GOL GLYCEROL × 5	X-RAY DIFFRACTION X-ray crystallization conditions pH 8；60 MM TRIS-HCL PH 8.0, 10 MM CACL2, 84 MM NACL, 20% GLYCEROL V/V, 17% PEG550 MME V/V	Resolution 1.50 Å R-free 0.168

12 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	SAMP_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–204； UniProt 20–223 Author chain B； PDBConstruct 1–204； UniProt 20–223 Author chain C； PDBConstruct 1–204； UniProt 20–223 Author chain D； PDBConstruct 1–204； UniProt 20–223 Author chain E； PDBConstruct 1–204； UniProt 20–223 Author chain F； PDBConstruct 1–204； UniProt 20–223 Author chain G； PDBConstruct 1–204； UniProt 20–223 Author chain H； PDBConstruct 1–204； UniProt 20–223 Author chain I； PDBConstruct 1–204； UniProt 20–223 Author chain J； PDBConstruct 1–204； UniProt 20–223

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	2a3x
Deposition date deposition_date	2005-06-27
Structure title title	Decameric crystal structure of human serum amyloid P-component bound to Bis-1,2-{[(Z)-2carboxy- 2-methyl-1,3-dioxane]- 5-yloxycarbonyl}-piperazine
Keywords keywords	multivalent ligand, serum amyloid, Metal Binding Protein; METAL BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	40.89 Å
Radius of gyration Rg (electron density) rg_electron	39.91 Å
Forward intensity I(0) i0	741525000.00
Molecular weight molecular_weight	234750.0 kDa
Excluded volume excluded_volume	297750 Å³
Envelope volume envelope_volume	397480 Å³
Hydration-shell volume shell_volume	79227 Å³
Envelope diameter envelope_diameter	117.9 Å
Shell Rg shell_rg	49.62 Å
Envelope Rg envelope_rg	38.14 Å
Shape Rg shape_rg	39.91 Å
Total Rg total_rg	40.40 Å
Total atoms total_atoms	16606
Residues n_residues	2040
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

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

Maximum dimension Dmax dmax	114.6 Å
Rg (real space) rg_real	40.55 Å
Rg uncertainty (real space) rg_real_error	0.44 Å
I(0) (real space) i0_real	7.4150e+08
I(0) uncertainty (real space) i0_real_error	1.0940e+07
Rg (reciprocal space) rg_reciprocal	40.89 Å
I(0) (reciprocal space) i0_reciprocal	741800000.0000
Solution quality estimate total_estimate	0.8850
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	58.8 Å
Skewness Skewness skewness	-0.155
Kurtosis Kurtosis kurtosis	-0.603
Angular range angular_range	— – 0.1950 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	212900000.0000
Real-space data points n_real_points	40
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.750

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Serum amyloid P-component
Molecular weight formula_weight	23282.5 kDa
Source method src_method	nat
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	16606

HTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV

Entity 2 Entity 2 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	20

Entity 3 Entity 3 non-polymer

Description description	BIS-1,2-{[(Z)-2CARBOXY-2-METHYL-1,3-DIOXANE]-5-YLOXYCARBONYL}-PIPERAZINE
Molecular weight formula_weight	462.4 kDa
Source method src_method	syn
Copy count entity_count	3

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7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_id	d2a3xa_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d2a3xb_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d2a3xc_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d2a3xd_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d2a3xe_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d2a3xf_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d2a3xg_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d2a3xh_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d2a3xi_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

Domain ID domain_id	d2a3xj_
Class class	b — All beta proteins
Fold Fold fold	b.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamily	b.29.1 — Concanavalin A-like lectins/glucanases
Family Family family	b.29.1.5 — Pentraxin (pentaxin)

CATH v4.4 (10 domains)

Domain ID domain_id	2a3xA00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2a3xB00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2a3xC00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2a3xD00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2a3xE00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2a3xF00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2a3xG00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2a3xH00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2a3xI00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

Domain ID domain_id	2a3xJ00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	120 — Jelly Rolls
Homologous superfamily homologous superfamily	200 —

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8. Citations (1)

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Unit-cell length a length_a	77.861 Å
Unit-cell length b length_b	95.054 Å
Unit-cell length c length_c	164.257 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	98.74 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	20

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	3.000 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.2309
R_work r_work	0.2281
R_free r_free	0.2822

fit	/app/data/saxs_computation/a3/2a3x/2a3x.fit
pddf	/app/data/pr_computation/a3/2a3x/2a3x.pr.out
profile	/app/data/saxs_computation/a3/2a3x/2a3x.dat