SAXSdb — 5v8z

▼

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

Endoplasmic reticulum resident protein 29

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Calmegin × 1 （E2RA18） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Calmegin × 1 （E2RA18） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

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

Calmegin

Canis lupus familiaris

UniProt E2RA18

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Endoplasmic reticulum resident protein 29 × 1 （P30040） water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Endoplasmic reticulum resident protein 29 × 1 （P30040） water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CLGN_CANLF
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 5–38； UniProt 327–360 Author chain D； PDBConstruct 5–38； UniProt 327–360

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	5v8z
Deposition date deposition_date	2017-03-22
Structure title title	Crystal structure of ERp29 D-domain in complex with the P-domain of calmegin
Keywords keywords	chaperone, protein binding, protein folding; CHAPERONE
Experimental Method method	X-RAY DIFFRACTION

▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

5v8z__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5v8z__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5v8z__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	16.57 Å
Rg (electron density)	15.66 Å
Total Rg	16.66 Å
Atom count	984
Residues	124
Excluded volume	17455 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5v8z__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5v8z__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. 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	A,C
Atom count atom_count	2014

GSLPVYDALAGEFIRASGVEARQALLKQGQDNLSSVKETQKKWAEQYLKIMGKILDQGEDFPASEMTRIARLIEKNKMSDGKKEELQKSLNILTAFQKKGAEKEEL

Source Source

Source organism organism	Homo sapiens
Common name common_name	Human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Calmegin
Molecular weight formula_weight	4342.6 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

GSHMDEPKFIPDPNAEKPDDWNEDMDGEWEAPRISNPA

Source Source

Source organism organism	Canis lupus familiaris
Common name common_name	Dog
NCBI taxonomy ID ncbi_taxonomy_id	9615
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	37

▼

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d5v8za1
Class class	a — All alpha proteins
Fold Fold fold	a.71 — ERP29 C domain-like
Superfamily Superfamily superfamily	a.71.1 — ERP29 C domain-like
Family Family family	a.71.1.1 — ERP29 C domain-like

Domain ID domain_id	d5v8za2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d5v8zc1
Class class	a — All alpha proteins
Fold Fold fold	a.71 — ERP29 C domain-like
Superfamily Superfamily superfamily	a.71.1 — ERP29 C domain-like
Family Family family	a.71.1.1 — ERP29 C domain-like

Domain ID domain_id	d5v8zc2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id	5v8zA00
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	5v8zC00
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

▶

Unit-cell length a length_a	67.782 Å
Unit-cell length b length_b	67.620 Å
Unit-cell length c length_c	73.492 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	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.105 Å
Low-resolution limit resolution_low	33.810 Å
R factor r_factor	0.2117
R_work r_work	0.2112
R_free r_free	0.2191

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

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

Calmegin

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5v8z__assembly_1__model_1

5v8z__assembly_1__model_1 | I(q)

5v8z__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

7. Citations (1)

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

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

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Calmegin

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

5v8z__assembly_1__model_1

5v8z__assembly_1__model_1 | I(q)

5v8z__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

7. Citations (1)