SAXSdb — 8hgg

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

Bone marrow proteoglycan

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–222 Chain B； UniProt 1–222	Not recorded	Pappalysin-1 × 2 （Q13219） ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.64 Å

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 8HGG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1H8U Crystal Structure of the Eosinophil Major Basic Protein at 1.8A: An Atypical Lectin with a Paradigm Shift in Specificity Deposited 2001-02-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 106–222（117 aa）	Not recorded	SO4 SULFATE ION × 5 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100MM MALONIC ACID PH6, 140MM POTTASIUM DIHYDROGEN PHOSPHATE., pH 6.00	Resolution 1.80 Å R-free 0.264
1H8U Crystal Structure of the Eosinophil Major Basic Protein at 1.8A: An Atypical Lectin with a Paradigm Shift in Specificity Deposited 2001-02-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 106–222（117 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；100MM MALONIC ACID PH6, 140MM POTTASIUM DIHYDROGEN PHOSPHATE., pH 6.00	Resolution 1.80 Å R-free 0.264
2BRS EMBP Heparin complex Deposited 2005-05-11	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 106–222（117 aa）	Not recorded	SO4 SULFATE ION × 5	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.291
2BRS EMBP Heparin complex Deposited 2005-05-11	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 106–222（117 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.291
4QXX Structure of the amyloid forming peptide GNLVS (residues 26-30) from the eosinophil major basic protein (EMBP) Deposited 2014-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain Z 131–135（5 aa） Fragment：GNLVS peptide (UNP residues 131-135)	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.2；291 K；2 M ammonium sulfate, 0.1 M phosphate/citrate, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 291K	Resolution 1.45 Å R-free 0.192
7Y5N Structure of 1:1 PAPP-A.ProMBP complex(half map) Deposited 2022-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–222（222 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ZN ZINC ION × 1 CA CALCIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.45 Å
9DKZ In situ microED structure of the Eosinophil major basic protein-1 Deposited 2024-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 107–222（116 aa）	Not recorded	No recorded non-water small molecule	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7；secretory granule matrix cryo-EM vitrification conditions Cryogen ETHANE；Blot time of 6~8 sec, single-side back blotting	Resolution 3.20 Å R-free 0.311
9PPV In situ MicroED structure of human eosinophil major basic protein-1 Deposited 2025-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 106–222（117 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å R-free 0.313
9PPV In situ MicroED structure of human eosinophil major basic protein-1 Deposited 2025-07-22	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 106–222（117 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å R-free 0.313
9PSE In situ MicroED structure of IL-5 activated human eosinophil major basic protein-1 Deposited 2025-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 107–222（116 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4；Harvested from human donor peripheral blood and rested in 1640 RPMI medium supplemented with 0.1% human serum albumin (HSA) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å R-free 0.320
9PSE In situ MicroED structure of IL-5 activated human eosinophil major basic protein-1 Deposited 2025-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 107–222（116 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4；Harvested from human donor peripheral blood and rested in 1640 RPMI medium supplemented with 0.1% human serum albumin (HSA) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å R-free 0.320
9PSK In situ MicroED structure of IL-33 activated human eosinophil major basic protein-1 Deposited 2025-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 106–222（117 aa）	Not recorded	No recorded non-water small molecule	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4；Harvested eosinophiles resting in 1640 RPMI medium (Sigma-Aldrich) supplemented with 0.1% human serum albumin (HSA) (Sigma-Aldrich) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å R-free 0.340
9PSK In situ MicroED structure of IL-33 activated human eosinophil major basic protein-1 Deposited 2025-07-25	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 106–222（117 aa）	Not recorded	CL CHLORIDE ION × 1	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 7.4；Harvested eosinophiles resting in 1640 RPMI medium (Sigma-Aldrich) supplemented with 0.1% human serum albumin (HSA) (Sigma-Aldrich) cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.18 Å R-free 0.340

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

View Construct and Data Evidence

UniProt name	PRG2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–222； UniProt 1–222 Author chain B； PDBConstruct 1–222； UniProt 1–222

Pappalysin-1

OrganismNot specified

UniProt Q13219

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain C； UniProt 1–1627 Chain D； UniProt 1–1627	Not recorded	Bone marrow proteoglycan × 2 （P13727） ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 3.64 Å

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 8HGG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7UFG Cryo-EM structure of PAPP-A in complex with IGFBP5 Deposited 2022-03-22	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 81–1627（1547 aa） Chain B 81–1627（1547 aa）	Mutation：E483A, S1144Y Mutation：E483A, S1144Y	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 9.2；BTP (Bis-Tris-Propane) pH 9.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.28 Å
7Y5N Structure of 1:1 PAPP-A.ProMBP complex(half map) Deposited 2022-06-17	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 81–1627（1547 aa） Chain D 81–1627（1547 aa）	Not recorded	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 10 ZN ZINC ION × 1 CA CALCIUM ION × 7	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.45 Å
7Y5Q Structure of 1:1 PAPP-A.STC2 complex(half map) Deposited 2022-06-17	Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 81–1627（1547 aa） Chain B 81–1627（1547 aa）	Not recorded	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8A7D Partial dimer complex of PAPP-A and its inhibitor STC2 Deposited 2022-06-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 82–1617（1536 aa） Chain Q 82–1617（1536 aa）	Mutation：E563Q Mutation：E563Q	NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ZN ZINC ION × 1 CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；Hepes buffer, 20 mM Hepes pH 7.4 100 mM NaCl, 1 mM CaCl cryo-EM vitrification conditions Cryogen ETHANE；4 s	Resolution 3.06 Å
8A7E PAPP-A dimer in complex with its inhibitor STC2 Deposited 2022-06-20	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 82–1617（1536 aa） Chain Q 82–1617（1536 aa）	Mutation：E563Q Mutation：E563Q	ZN ZINC ION × 2 CA CALCIUM ION × 16	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；HEPES buffer 20 mM Hepes pH 7.5 100 mM NaCl, 1mM CaCl cryo-EM vitrification conditions Cryogen ETHANE；Blot time 4.5 sec	Resolution 5.02 Å
8D8O Cryo-EM structure of substrate unbound PAPP-A Deposited 2022-06-08	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 81–1627（1547 aa） Chain B 81–1627（1547 aa）	Mutation：E483A, S1144Y Mutation：E483A, S1144Y	ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 9.2；BTP (Bis-Tris-Propane) pH 9.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.35 Å
8HGH Structure of 2:2 PAPP-A.STC2 complex Deposited 2022-11-14	Different construct Different oligomeric state Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 81–1627（1547 aa） Chain B 81–1627（1547 aa）	Not recorded	ZN ZINC ION × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.16 Å

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PAPP1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain C； PDBConstruct 1–1627； UniProt 1–1627 Author chain D； PDBConstruct 1–1627； UniProt 1–1627

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	8hgg
Deposition date deposition_date	2022-11-14
Structure title title	Structure of 2:2 PAPP-A.ProMBP complex
Keywords keywords	Hydrolase, METAL BINDING PROTEIN, Complex; HYDROLASE
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	60.09 Å
Radius of gyration Rg (electron density) rg_electron	60.29 Å
Forward intensity I(0) i0	2016050000.00
Molecular weight molecular_weight	362130.0 kDa
Excluded volume excluded_volume	446090 Å³
Envelope volume envelope_volume	735350 Å³
Hydration-shell volume shell_volume	100580 Å³
Envelope diameter envelope_diameter	233.4 Å
Shell Rg shell_rg	63.74 Å
Envelope Rg envelope_rg	59.18 Å
Shape Rg shape_rg	60.24 Å
Total Rg total_rg	60.55 Å
Total atoms total_atoms	25404
Residues n_residues	3238
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	211.2 Å
Rg (real space) rg_real	60.27 Å
Rg uncertainty (real space) rg_real_error	1.90 Å
I(0) (real space) i0_real	2.0160e+09
I(0) uncertainty (real space) i0_real_error	4.3460e+07
Rg (reciprocal space) rg_reciprocal	59.91 Å
I(0) (reciprocal space) i0_reciprocal	2015000000.0000
Solution quality estimate total_estimate	0.8698
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	65.0 Å
Skewness Skewness skewness	0.393
Kurtosis Kurtosis kurtosis	-0.329
Angular range angular_range	— – 0.1300 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	179300000.0000
Real-space data points n_real_points	27
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.814; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.864

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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	Bone marrow proteoglycan
Molecular weight formula_weight	25236.6 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	25404

MKLPLLLALLFGAVSALHLRSETSTFETPLGAKTLPEDEETPEQEMEETPCRELEEEEEWGSGSEDASKKDGAVESISVPDMVDKNLTCPEEEDTVKVVGIPGCQTCRYLLVRSLQTFSQAWFTCRRCYRGNLVSIHNFNINYRIQCSVSALNQGQVWIGGRITGSGRCRRFQWVDGSRWNFAYWAAHQPWSRGGHCVALCTRGGHWRRAHCLRRLPFICSY

Entity 2 Entity 2 polymer

Description description	Pappalysin-1
Molecular weight formula_weight	181175.6 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

MRLWSWVLHLGLLSAALGCGLAERPRRARRDPRAGRPPRPAAGPATCATRAARGRRASPPPPPPPGGAWEAVRVPRRRQQREARGATEEPSPPSRALYFSGRGEQLRLRADLELPRDAFTLQVWLRAEGGQRSPAVITGLYDKCSYISRDRGWVVGIHTISDQDNKDPRYFFSLKTDRARQVTTINAHRSYLPGQWVYLAATYDGQFMKLYVNGAQVATSGEQVGGIFSPLTQKCKVLMLGGSALNHNYRGYIEHFSLWKVARTQREILSDMETHGAHTALPQLLLQENWDNVKHAWSPMKDGSSPKVEFSNAHGFLLDTSLEPPLCGQTLCDNTEVIASYNQLSSFRQPKVVRYRVVNLYEDDHKNPTVTREQVDFQHHQLAEAFKQYNISWELDVLEVSNSSLRRRLILANCDISKIGDENCDPECNHTLTGHDGGDCRHLRHPAFVKKQHNGVCDMDCNYERFNFDGGECCDPEITNVTQTCFDPDSPHRAYLDVNELKNILKLDGSTHLNIFFAKSSEEELAGVATWPWDKEALMHLGGIVLNPSFYGMPGHTHTMIHEIGHSLGLYHVFRGISEIQSCSDPCMETEPSFETGDLCNDTNPAPKHKSCGDPGPGNDTCGFHSFFNTPYNNFMSYADDDCTDSFTPNQVARMHCYLDLVYQGWQPSRKPAPVALAPQVLGHTTDSVTLEWFPPIDGHFFERELGSACHLCLEGRILVQYASNASSPMPCSPSGHWSPREAEGHPDVEQPCKSSVRTWSPNSAVNPHTVPPACPEPQGCYLELEFLYPLVPESLTIWVTFVSTDWDSSGAVNDIKLLAVSGKNISLGPQNVFCDVPLTIRLWDVGEEVYGIQIYTLDEHLEIDAAMLTSTADTPLCLQCKPLKYKVVRDPPLQMDVASILHLNRKFVDMDLNLGSVYQYWVITISGTEESEPSPAVTYIHGSGYCGDGIIQKDQGEQCDDMNKINGDGCSLFCRQEVSFNCIDEPSRCYFHDGDGVCEEFEQKTSIKDCGVYTPQGFLDQWASNASVSHQDQQCPGWVIIGQPAASQVCRTKVIDLSEGISQHAWYPCTISYPYSQLAQTTFWLRAYFSQPMVAAAVIVHLVTDGTYYGDQKQETISVQLLDTKDQSHDLGLHVLSCRNNPLIIPVVHDLSQPFYHSQAVRVSFSSPLVAISGVALRSFDNFDPVTLSSCQRGETYSPAEQSCVHFACEKTDCPELAVENASLNCSSSDRYHGAQCTVSCRTGYVLQIRRDDELIKSQTGPSVTVTCTEGKWNKQVACEPVDCSIPDHHQVYAASFSCPEGTTFGSQCSFQCRHPAQLKGNNSLLTCMEDGLWSFPEALCELMCLAPPPVPNADLQTARCRENKHKVGSFCKYKCKPGYHVPGSSRKSKKRAFKTQCTQDGSWQEGACVPVTCDPPPPKFHGLYQCTNGFQFNSECRIKCEDSDASQGLGSNVIHCRKDGTWNGSFHVCQEMQGQCSVPNELNSNLKLQCPDGYAIGSECATSCLDHNSESIILPMNVTVRDIPHWLNPTRVERVVCTAGLKWYPHPALIHCVKGCEPFMGDNYCDAINNRAFCNYDGGDCCTSTVKTKKVTPFPMSCDLQGDCACRDPQAQEHSRKDLRGYSHG

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	2

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8. Citations (1)

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Resolution resolution	3.64 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	261371

fit	/app/data/saxs_computation/hg/8hgg/8hgg.fit
pddf	/app/data/pr_computation/hg/8hgg/8hgg.pr.out
profile	/app/data/saxs_computation/hg/8hgg/8hgg.dat

Structure of 2:2 PAPP-A.ProMBP complex

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

Bone marrow proteoglycan

State in the Current Structure

Other States of the Same Protein in the Database

Pappalysin-1

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

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)