3nh7

Crystal structure of the neutralizing Fab fragment AbD1556 bound to the BMP type I receptor IA

Method: X-RAY DIFFRACTION D_max: 146.1 Å Quality: GOOD

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

Bone morphogenetic protein receptor type-1A

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 24–152	Fragment：extracellular domain, UNP residues 24-152	Antibody fragment Fab AbD1556, heavy chain × 1 Antibody fragment Fab AbD1556, light chain × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；100mM Tris-HCl pH 7.0, 20% (w/v) PEG 8000 and 10% (w/v) glucose , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.280
2	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 24–152	Fragment：extracellular domain, UNP residues 24-152	Antibody fragment Fab AbD1556, heavy chain × 1 Antibody fragment Fab AbD1556, light chain × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；100mM Tris-HCl pH 7.0, 20% (w/v) PEG 8000 and 10% (w/v) glucose , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.280
3	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain C； UniProt 24–152	Fragment：extracellular domain, UNP residues 24-152	Antibody fragment Fab AbD1556, heavy chain × 1 Antibody fragment Fab AbD1556, light chain × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；100mM Tris-HCl pH 7.0, 20% (w/v) PEG 8000 and 10% (w/v) glucose , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.280
4	Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 24–152	Fragment：extracellular domain, UNP residues 24-152	Antibody fragment Fab AbD1556, heavy chain × 1 Antibody fragment Fab AbD1556, light chain × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；294 K；100mM Tris-HCl pH 7.0, 20% (w/v) PEG 8000 and 10% (w/v) glucose , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.70 Å R-free 0.280

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 3NH7	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1ES7 COMPLEX BETWEEN BMP-2 AND TWO BMP RECEPTOR IA ECTODOMAINS Deposited 2000-04-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 55–143（89 aa） Fragment：EXTRACELLULAR DOMAIN Chain D 55–143（89 aa） Fragment：EXTRACELLULAR DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；296 K；sodium acetate, imidazole, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 296K	Resolution 2.90 Å R-free 0.229
1REW Structural refinement of the complex of bone morphogenetic protein 2 and its type IA receptor Deposited 2003-11-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain Chain D 24–152（129 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；280 K；sodium acetate, imidazole, glucose, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 280K	Resolution 1.86 Å R-free 0.229
2GOO Ternary Complex of BMP-2 bound to BMPR-Ia-ECD and ActRII-ECD Deposited 2006-04-13	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 B 24–152（129 aa） Fragment：Residues 24-152 Chain E 24–152（129 aa） Fragment：Residues 24-152	Not recorded	NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；4M sodium formate, 100mM Hepes, 3% dioxane, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.20 Å R-free 0.259
2H62 Crystal structure of a ternary ligand-receptor complex of BMP-2 Deposited 2006-05-30	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.75；294 K；50% PPG400, 0.1M Bis-Tris, pH 5.75, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 1.85 Å R-free 0.225
2H64 Crystal structure of a ternary ligand-receptor complex of BMP-2 Deposited 2006-05-30	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 24–152（129 aa） Fragment：extracellular domain	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.75；294 K；30% PEG3350, 0.1M Tris-HCl pH 8.75, 0.2M NH4CH3COO, VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 1.92 Å R-free 0.264
2K3G NMR structure analysis of a BMP receptor Deposited 2008-05-07	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 51–152（102 aa） Fragment：Extracellular domain (UNP residues 51-152)	Mutation：A28G	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.3；298 K；Pressure ambient NMR sample composition 1.1 mM [U-99% 15N] Bone Morphogenetic Protein Receptor Type IA, 10 mM potassium phosphate, 0.2 w/v sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.5 mM [U-94% 13C; U-98% 15N] Bone Morphogenetic Protein Receptor Type IA, 10 mM potassium phosphate, 0.2 w/v sodium azide, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2QJ9 Crystal structure analysis of BMP-2 in complex with BMPR-IA variant B1 Deposited 2007-07-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain (residues 24-152) Chain D 24–152（129 aa） Fragment：extracellular domain (residues 24-152)	Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；0.8M K Na phosphate, 25% ethylene glycol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.44 Å R-free 0.253
2QJA Crystal structure analysis of BMP-2 in complex with BMPR-IA variant B12 Deposited 2007-07-06	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain (residues 24-152) Chain D 24–152（129 aa） Fragment：extracellular domain (residues 24-152)	Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S,A74T,M78L,K79G,Y80L Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S,A74T,M78L,K79G,Y80L	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；0.8M K Na phosphate, 25% ethylene glycol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.60 Å R-free 0.254
2QJB Crystal structure analysis of BMP-2 in complex with BMPR-IA variant IA/IB Deposited 2007-07-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 24–152（129 aa） Fragment：extracellular domain (residues 24-152) Chain D 24–152（129 aa） Fragment：extracellular domain (residues 24-152)	Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S,A74T,M78L,K79G,Y80L,D46E,G42H,A61T,I62M Mutation：K88R,S90T,K92I,A93P,Q94H,L95Q,T98S,A74T,M78L,K79G,Y80L,D46E,G42H,A61T,I62M	CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；298 K；0.8M K Na phosphate, 25% ethylene glycol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.50 Å R-free 0.263
3QB4 Crystal structure of a TGF-beta ligand-receptor complex Deposited 2011-01-12	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–152（129 aa） Fragment：BMP receptor BMPR-IA, residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；0.1M Hepes pH 7.5, 0.2M NaCl 20% (w/v) PEG3350 , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.28 Å R-free 0.241
3QB4 Crystal structure of a TGF-beta ligand-receptor complex Deposited 2011-01-12	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 24–152（129 aa） Fragment：BMP receptor BMPR-IA, residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；0.1M Hepes pH 7.5, 0.2M NaCl 20% (w/v) PEG3350 , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.28 Å R-free 0.241
3QB4 Crystal structure of a TGF-beta ligand-receptor complex Deposited 2011-01-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 24–152（129 aa） Fragment：BMP receptor BMPR-IA, residues 24-152 Chain D 24–152（129 aa） Fragment：BMP receptor BMPR-IA, residues 24-152	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；294 K；0.1M Hepes pH 7.5, 0.2M NaCl 20% (w/v) PEG3350 , VAPOR DIFFUSION, HANGING DROP, temperature 294K	Resolution 2.28 Å R-free 0.241

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

View Construct and Data Evidence

UniProt name	BMR1A_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain A； PDBConstruct 1–129； UniProt 24–152 Author chain B； PDBConstruct 1–129； UniProt 24–152 Author chain C； PDBConstruct 1–129； UniProt 24–152 Author chain D； PDBConstruct 1–129； UniProt 24–152

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	3nh7
Deposition date deposition_date	2010-06-14
Structure title title	Crystal structure of the neutralizing Fab fragment AbD1556 bound to the BMP type I receptor IA
Keywords keywords	Antibody-antigen complex, BMP receptor extracellular domain, Bone morphogenetic protein, IMMUNE SYSTEM; IMMUNE SYSTEM
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	45.28 Å
Radius of gyration Rg (electron density) rg_electron	44.86 Å
Forward intensity I(0) i0	739576000.00
Molecular weight molecular_weight	218130.0 kDa
Excluded volume excluded_volume	270260 Å³
Envelope volume envelope_volume	388650 Å³
Hydration-shell volume shell_volume	72531 Å³
Envelope diameter envelope_diameter	149.2 Å
Shell Rg shell_rg	49.66 Å
Envelope Rg envelope_rg	43.91 Å
Shape Rg shape_rg	44.82 Å
Total Rg total_rg	45.20 Å
Total atoms total_atoms	15323
Residues n_residues	2038
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	146.1 Å
Rg (real space) rg_real	45.16 Å
Rg uncertainty (real space) rg_real_error	1.14 Å
I(0) (real space) i0_real	7.3960e+08
I(0) uncertainty (real space) i0_real_error	1.3800e+07
Rg (reciprocal space) rg_reciprocal	45.28 Å
I(0) (reciprocal space) i0_reciprocal	739700000.0000
Solution quality estimate total_estimate	0.8973
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	54.3 Å
Skewness Skewness skewness	0.211
Kurtosis Kurtosis kurtosis	-0.544
Angular range angular_range	— – 0.1750 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	50120000.0000
Real-space data points n_real_points	36
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.869

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Antibody fragment Fab AbD1556, heavy chain
Molecular weight formula_weight	25153.0 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,I,J,K
Atom count atom_count	15350

QVQLVESGGGLVQPGGSLRLSCAASGFTFSNYTLNWVRQAPGKGLEWVSYTSSSGSLTGYADSVKGRFTISRDNSKNTLYLQMNSLRAEDTAVYYCARERWHVRGYFDHWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSEFSAWSHPQFEK

来源 Source

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

Entity 2 Entity 2 polymer

Description description	Antibody fragment Fab AbD1556, light chain
Molecular weight formula_weight	22488.8 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L,M,N,O

DIELTQPPSVSVAPGQTARISCSGDSLGSKYVIWYQQKPGQAPVLVIYDDSNRPSGIPERFSGSNSGNTATLTISGTQAEDEADYYCSTFTMSGNGTVFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTEA

来源 Source

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

Entity 3 Entity 3 polymer

Description description	Bone morphogenetic protein receptor type-1A
Molecular weight formula_weight	14199.9 kDa
EC 编号 ec_number	2.7.11.30
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

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

QNLDSMLHGTGMKSDSDQKKSENGVTLAPEDTLPFLKCYCSGHCPDDAINNTCITNGHCFAIIEEDDQGETTLASGCMKYEGSDFQCKDSPKAQLRRTIECCRTNLCNQYLQPTLPPVVIGPFFDGSIR

来源 Source

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

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	27

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7. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (16 domains)

Domain ID domain_id	d3nh7a_
Class class	g — Small proteins
Fold Fold fold	g.7 — Snake toxin-like
Superfamily Superfamily superfamily	g.7.1 — Snake toxin-like
Family Family family	g.7.1.3 — Extracellular domain of cell surface receptors

Domain ID domain_id	d3nh7b_
Class class	g — Small proteins
Fold Fold fold	g.7 — Snake toxin-like
Superfamily Superfamily superfamily	g.7.1 — Snake toxin-like
Family Family family	g.7.1.3 — Extracellular domain of cell surface receptors

Domain ID domain_id	d3nh7c_
Class class	g — Small proteins
Fold Fold fold	g.7 — Snake toxin-like
Superfamily Superfamily superfamily	g.7.1 — Snake toxin-like
Family Family family	g.7.1.3 — Extracellular domain of cell surface receptors

Domain ID domain_id	d3nh7d_
Class class	g — Small proteins
Fold Fold fold	g.7 — Snake toxin-like
Superfamily Superfamily superfamily	g.7.1 — Snake toxin-like
Family Family family	g.7.1.3 — Extracellular domain of cell surface receptors

Domain ID domain_id	d3nh7h_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d3nh7i_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d3nh7j_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d3nh7k_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d3nh7l1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3nh7l2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3nh7m1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3nh7m2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3nh7n1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3nh7n2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3nh7o1
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

Domain ID domain_id	d3nh7o2
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.0 — automated matches

CATH v4.4 (20 domains)

Domain ID domain_id	3nh7A00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	60 — CD59
Homologous superfamily homologous superfamily	10 — CD59

Domain ID domain_id	3nh7B00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	60 — CD59
Homologous superfamily homologous superfamily	10 — CD59

Domain ID domain_id	3nh7C00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	60 — CD59
Homologous superfamily homologous superfamily	10 — CD59

Domain ID domain_id	3nh7D00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	60 — CD59
Homologous superfamily homologous superfamily	10 — CD59

Domain ID domain_id	3nh7H01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7H02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7I01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7I02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7J01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7J02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7K01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7K02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7L01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7L02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7M01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7M02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7N01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7N02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7O01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	3nh7O02
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

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8. Citations (1)

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Unit-cell length a length_a	89.320 Å
Unit-cell length b length_b	129.255 Å
Unit-cell length c length_c	100.239 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.27 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

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

Resolution resolution	2.700 Å
Low-resolution limit resolution_low	30.400 Å
R factor r_factor	0.2364
R_work r_work	0.2341
R_free r_free	0.2804

Crystal structure of the neutralizing Fab fragment AbD1556 bound to the BMP type I receptor IA

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

Bone morphogenetic protein receptor type-1A

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

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 water

7. Fold Classification (SCOP + CATH) 36 domains

SCOP 2.08 (16 domains)

CATH v4.4 (20 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/nh/3nh7/3nh7.fit
pddf	/app/data/pr_computation/nh/3nh7/3nh7.pr.out
profile	/app/data/saxs_computation/nh/3nh7/3nh7.dat