SAXSdb — 5v90

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

Endoplasmic reticulum resident protein 29

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 158–261	Fragment：UNP residues 158-261	Calreticulin × 1 （P27797）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；2.0 M ammonium sulfate, 0.1 M HEPES pH 7.5	Resolution 3.25 Å R-free 0.262
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 158–261	Fragment：UNP residues 158-261	Calreticulin × 1 （P27797） GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；2.0 M ammonium sulfate, 0.1 M HEPES pH 7.5	Resolution 3.25 Å R-free 0.262

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 5V90	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2QC7 Crystal structure of the protein-disulfide isomerase related chaperone ERp29 Deposited 2007-06-19	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 34–261（228 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；10 mg/ml protein in 5 mM HEPES, pH 7.5, 25 mM NaCl, 0.0025% (v/v) beta-mercaptoethanol was equlibrated with a reservoir containing 0.45 M (NH4)2SO4, 0.1 M sodium acetate buffer, pH 4.5 and 18-20% (w/v) PEG 2000 monomethyl ether. Crystals of about 0.1 mm in size grew in two days. , VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.90 Å R-free 0.279
2QC7 Crystal structure of the protein-disulfide isomerase related chaperone ERp29 Deposited 2007-06-19	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain B 34–261（228 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；10 mg/ml protein in 5 mM HEPES, pH 7.5, 25 mM NaCl, 0.0025% (v/v) beta-mercaptoethanol was equlibrated with a reservoir containing 0.45 M (NH4)2SO4, 0.1 M sodium acetate buffer, pH 4.5 and 18-20% (w/v) PEG 2000 monomethyl ether. Crystals of about 0.1 mm in size grew in two days. , VAPOR DIFFUSION, HANGING DROP, temperature 277K	Resolution 2.90 Å R-free 0.279
5V8Z Crystal structure of ERp29 D-domain in complex with the P-domain of calmegin Deposited 2017-03-22	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 158–261（104 aa） Fragment：UNP residues 158-261	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；1.4 M sodium citrate pH 7.5	Resolution 2.10 Å R-free 0.219
5V8Z Crystal structure of ERp29 D-domain in complex with the P-domain of calmegin Deposited 2017-03-22	Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 158–261（104 aa） Fragment：UNP residues 158-261	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；1.4 M sodium citrate pH 7.5	Resolution 2.10 Å R-free 0.219

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ERP29_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–106； UniProt 158–261 Author chain C； PDBConstruct 3–106； UniProt 158–261

Calreticulin

Homo sapiens

UniProt P27797

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 D； UniProt 238–273	Fragment：UNP residues 238-273	Endoplasmic reticulum resident protein 29 × 1 （P30040）	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；2.0 M ammonium sulfate, 0.1 M HEPES pH 7.5	Resolution 3.25 Å R-free 0.262
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 238–273	Fragment：UNP residues 238-273	Endoplasmic reticulum resident protein 29 × 1 （P30040） GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；2.0 M ammonium sulfate, 0.1 M HEPES pH 7.5	Resolution 3.25 Å R-free 0.262

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 5V90	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2CLR THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE Deposited 1994-08-01	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–10（10 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
2CLR THREE DIMENSIONAL STRUCTURE OF A PEPTIDE EXTENDING OUT ONE END OF A CLASS I MHC BINDING SITE Deposited 1994-08-01	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain F 1–10（10 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
3DOW Complex structure of GABA type A receptor associated protein and its binding epitope on calreticulin Deposited 2008-07-07	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 195–205（11 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；0.1 M MES, 27% v/v PEG MME 550, 10 mM ZnSO4, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K	Resolution 2.30 Å R-free 0.270
3POS Crystal structure of the globular domain of human calreticulin Deposited 2010-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–204（187 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG Chain A 302–368（67 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.1 K；30% PEG 4000, 0.1M sodium acetate, 0.1M Tris, pH 8.5-9, VAPOR DIFFUSION, HANGING DROP, temperature 277.1K	Resolution 1.65 Å R-free 0.205
3POS Crystal structure of the globular domain of human calreticulin Deposited 2010-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 18–204（187 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG Chain B 302–368（67 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.1 K；30% PEG 4000, 0.1M sodium acetate, 0.1M Tris, pH 8.5-9, VAPOR DIFFUSION, HANGING DROP, temperature 277.1K	Resolution 1.65 Å R-free 0.205
3POS Crystal structure of the globular domain of human calreticulin Deposited 2010-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain C 18–204（187 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG Chain C 302–368（67 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.1 K；30% PEG 4000, 0.1M sodium acetate, 0.1M Tris, pH 8.5-9, VAPOR DIFFUSION, HANGING DROP, temperature 277.1K	Resolution 1.65 Å R-free 0.205
3POW Crystal structure of the globular domain of human calreticulin Deposited 2010-11-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–204（187 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG Chain A 302–368（67 aa） Fragment：Globular domain, UNP residues 18-204 and 302-368 linked with GSG	Not recorded	CA CALCIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6；277.1 K；30% PEG 4000, 0.2M ammonium acetate, 10mM magnesium acetate, and either 0.05M MES (pH 5.7 or 6.0), or 0.05M HEPES (pH 7.0), VAPOR DIFFUSION, temperature 277.1K	Resolution 1.55 Å R-free 0.191
5LK5 Crystal structure of the globular domain of human calreticulin mutant D71K Deposited 2016-07-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric	Chain A 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain A 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain B 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain B 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain C 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain C 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain D 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain D 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain E 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain E 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain F 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain F 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain G 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain G 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain H 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain H 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain I 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain I 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain J 18–204（187 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368 Chain J 303–368（66 aa） Fragment：UNP residues 18-204,UNP residues 303-368,UNP residues 18-204,UNP residues 303-368	Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K Mutation：D71K,D71K,D71K,D71K	CA CALCIUM ION × 10 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；30% PEG4000 0.2 M MgCl2 0.1 M Tris-HCl	Resolution 2.30 Å R-free 0.247
6ENY Structure of the human PLC editing module Deposited 2017-10-07	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain G 18–417（400 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 5.80 Å
7QPD Structure of the human MHC I peptide-loading complex editing module Deposited 2022-01-03	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric	Chain C 18–417（400 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.73 Å
8TZO Structure of human Wnt7a bound to WLS and CALR Deposited 2023-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–417（417 aa）	Not recorded	PAM PALMITOLEIC ACID × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1 CA CALCIUM ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8TZR Structure of human Wnt3a bound to WLS and CALR Deposited 2023-08-27	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–417（417 aa）	Not recorded	PAM PALMITOLEIC ACID × 1 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å

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

View Construct and Data Evidence

UniProt name	CALR_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 5–40； UniProt 238–273 Author chain D； PDBConstruct 5–40； UniProt 238–273

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	5v90
Deposition date deposition_date	2017-03-22
Structure title title	Crystal structure of ERp29 D-domain in complex with the P-domain of calreticulin
Keywords keywords	chaperone, protein binding, protein folding; CHAPERONE
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	19.80 Å
Radius of gyration Rg (electron density) rg_electron	18.93 Å
Forward intensity I(0) i0	12779700.00
Molecular weight molecular_weight	26457.0 kDa
Excluded volume excluded_volume	33044 Å³
Envelope volume envelope_volume	39633 Å³
Hydration-shell volume shell_volume	17943 Å³
Envelope diameter envelope_diameter	61.9 Å
Shell Rg shell_rg	24.48 Å
Envelope Rg envelope_rg	19.12 Å
Shape Rg shape_rg	18.89 Å
Total Rg total_rg	19.93 Å
Total atoms total_atoms	3447
Residues n_residues	243
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	62.4 Å
Rg (real space) rg_real	19.69 Å
Rg uncertainty (real space) rg_real_error	0.36 Å
I(0) (real space) i0_real	1.2780e+07
I(0) uncertainty (real space) i0_real_error	1.4220e+05
Rg (reciprocal space) rg_reciprocal	19.70 Å
I(0) (reciprocal space) i0_reciprocal	12780000.0000
Solution quality estimate total_estimate	0.9018
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	26.4 Å
Skewness Skewness skewness	0.155
Kurtosis Kurtosis kurtosis	-0.474
Angular range angular_range	— – 0.4000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4393000.0000
Real-space data points n_real_points	72
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.988

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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	Endoplasmic reticulum resident protein 29
Molecular weight formula_weight	11903.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,A
Atom count atom_count	3448

GSLPVYDALAGEFIRASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGKKEELQKSLNILTAFQKKGAEKEEL

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	Calreticulin
Molecular weight formula_weight	4665.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

GSHMKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKG

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 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	5v90A00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1150 — Endoplasmic reticulum protein erp29
Homologous superfamily homologous superfamily	12 — Endoplasmic reticulum resident protein 29, C-terminal domain

Domain ID domain_id	5v90C00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1150 — Endoplasmic reticulum protein erp29
Homologous superfamily homologous superfamily	12 — Endoplasmic reticulum resident protein 29, C-terminal domain

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8. Citations (1)

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Unit-cell length a length_a	68.573 Å
Unit-cell length b length_b	68.573 Å
Unit-cell length c length_c	167.778 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	16

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	3.255 Å
Low-resolution limit resolution_low	43.340 Å
R factor r_factor	0.2413
R_work r_work	0.2401
R_free r_free	0.2621

fit	/app/data/saxs_computation/v9/5v90/5v90.fit
pddf	/app/data/pr_computation/v9/5v90/5v90.pr.out
profile	/app/data/saxs_computation/v9/5v90/5v90.dat

Crystal structure of ERp29 D-domain in complex with the P-domain of calreticulin

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

Endoplasmic reticulum resident protein 29

State in the Current Structure

Other States of the Same Protein in the Database

Calreticulin

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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)