SAXSdb — 1bv8

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

ALPHA-2-MACROGLOBULIN

Homo sapiens

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1337–1474	Fragment：RECEPTOR BINDING DOMAIN	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5.1；298 K；Ionic strength (raw mmCIF value) 0.4；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 1BV8	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AYO RECEPTOR BINDING DOMAIN OF BOVINE ALPHA-2-MACROGLOBULIN Deposited 1997-11-07	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1338–1468（131 aa） Fragment：RECEPTOR-BINDING DOMAIN Chain B 1338–1468（131 aa） Fragment：RECEPTOR-BINDING DOMAIN	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.9；38% PEGMMES 2000, 25 MM CACL2, 100 MM HEPES, PH 6.9	Resolution 1.90 Å R-free 0.239
2P9R Human alpha2-macroglogulin is composed of multiple domains, as predicted by homology with complement component C3 Deposited 2007-03-26	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 126–227（102 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；295 K；11% PEG 3350, 200mM di-ammonium hydrogen citrate, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.30 Å R-free 0.281
2P9R Human alpha2-macroglogulin is composed of multiple domains, as predicted by homology with complement component C3 Deposited 2007-03-26	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 126–227（102 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；295 K；11% PEG 3350, 200mM di-ammonium hydrogen citrate, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.30 Å R-free 0.281
6TAV Crystal structure of endopeptidase-induced alpha2-macroglobulin Deposited 2019-10-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1474（1474 aa） Chain B 1–1474（1474 aa） Chain C 1–1474（1474 aa） Chain D 1–1474（1474 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 11	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Equivolumetric drops consisting of 0.2M tribasic ammonium citrate, pH6.4, 15% (w/v) polyethylene glycol 3350, plus 0.05M sodium fluoride as an additive, and protein solution at 4.9 absorption units at lambda=280nm yielded a single large well-shaped monocrystal after several months. This crystal could not be reproduced despite extensive trials.	Resolution 4.20 Å R-free 0.282
7O7L (h-alpha2M)4 native I Deposited 2021-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1474（1474 aa） Chain B 1–1474（1474 aa） Chain C 1–1474（1474 aa） Chain D 1–1474（1474 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.50 Å
7O7M (h-alpha2M)4 native II Deposited 2021-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1474（1474 aa） Chain B 1–1474（1474 aa） Chain C 1–1474（1474 aa） Chain D 1–1474（1474 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 6.60 Å
7O7N (h-alpha2M)4 semiactivated I state Deposited 2021-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1474（1474 aa） Chain B 1–1474（1474 aa） Chain C 1–1474（1474 aa） Chain D 1–1474（1474 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 7.30 Å
7O7O (h-alpha2M)4 semiactivated II state Deposited 2021-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1474（1474 aa） Chain B 1–1474（1474 aa） Chain C 1–1474（1474 aa） Chain D 1–1474（1474 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.80 Å
7O7P (h-alpha2M)4 activated state Deposited 2021-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1474（1474 aa） Chain B 1–1474（1474 aa） Chain C 1–1474（1474 aa） Chain D 1–1474（1474 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.60 Å
7O7Q (h-alpha2M)4 trypsin-activated state Deposited 2021-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1474（1474 aa） Chain B 1–1474（1474 aa） Chain C 1–1474（1474 aa） Chain D 1–1474（1474 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
7O7R (h-alpha2M)4 plasmin-activated I state Deposited 2021-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1474（1474 aa） Chain B 1–1474（1474 aa） Chain C 1–1474（1474 aa） Chain D 1–1474（1474 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
7O7S (h-alpha2M)4 plasmin-activated II state Deposited 2021-04-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–1474（1474 aa） Chain B 1–1474（1474 aa） Chain C 1–1474（1474 aa） Chain D 1–1474（1474 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.30 Å
7VON Native alpha-2-macroglobulin monomer Deposited 2021-10-14	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–1468（1442 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.20 Å
7VOO Induced alpha-2-macroglobulin monomer Deposited 2021-10-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–1335（1309 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å

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

View Construct and Data Evidence

UniProt name	A2MG_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–138； UniProt 1337–1474

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	1bv8
Deposition date deposition_date	1998-09-22
Structure title title	RECEPTOR DOMAIN FROM ALPHA-2-MACROGLOBULIN
Keywords keywords	PROTEINASE, PROTEIN BINDING; PROTEIN BINDING
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	17.59 Å
Radius of gyration Rg (electron density) rg_electron	16.55 Å
Forward intensity I(0) i0	4410080.00
Molecular weight molecular_weight	15433.0 kDa
Excluded volume excluded_volume	19414 Å³
Envelope volume envelope_volume	20204 Å³
Hydration-shell volume shell_volume	11579 Å³
Envelope diameter envelope_diameter	61.8 Å
Shell Rg shell_rg	20.48 Å
Envelope Rg envelope_rg	16.26 Å
Shape Rg shape_rg	16.44 Å
Total Rg total_rg	17.56 Å
Total atoms total_atoms	1985
Residues n_residues	137
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	60.3 Å
Rg (real space) rg_real	17.64 Å
Rg uncertainty (real space) rg_real_error	0.42 Å
I(0) (real space) i0_real	4.4100e+06
I(0) uncertainty (real space) i0_real_error	5.0680e+04
Rg (reciprocal space) rg_reciprocal	17.64 Å
I(0) (reciprocal space) i0_reciprocal	4410000.0000
Solution quality estimate total_estimate	0.7803
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	3
Primary peak position r_peak_primary	16.9 Å
Skewness Skewness skewness	0.403
Kurtosis Kurtosis kurtosis	-0.297
Angular range angular_range	— – 0.4500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	902900.0000
Real-space data points n_real_points	76
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.761; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.856; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bv8a_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.29 — Macroglobulin
Family Family family	b.1.29.1 — Alpha-macroglobulin receptor domain

CATH v4.4 (1 domains)

Domain ID domain_id	1bv8A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	690 — Alpha-macroglobulin, receptor-binding domain

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8. Citations (1)

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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	—

Description description	ALPHA-2-MACROGLOBULIN
Molecular weight formula_weight	15367.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1986

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

RECEPTOR DOMAIN FROM ALPHA-2-MACROGLOBULIN

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

ALPHA-2-MACROGLOBULIN

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 (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/bv/1bv8/1bv8.fit
pddf	/app/data/pr_computation/bv/1bv8/1bv8.pr.out
profile	/app/data/saxs_computation/bv/1bv8/1bv8.dat