SAXSdb — 1smr

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

RENIN

Mus musculus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	INHIBITOR CH-66 × 1 water × 2	Consistent with protein count
10	Protein homooligomer	Homooligomer	Protein 4	water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	INHIBITOR CH-66 × 1 water × 1	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	INHIBITOR CH-66 × 1	Consistent with protein count
4	Protein monomer	Monomer	Protein 1	No other associated polymer	Consistent with protein count
6	Protein heterocomplex	Heteromer	Protein 8	INHIBITOR CH-66 × 4 water × 3	Consistent with protein count
7	Protein heterocomplex	Heteromer	Protein 4	INHIBITOR CH-66 × 2 water × 3	Consistent with protein count
8	Protein heterocomplex	Heteromer	Protein 4	INHIBITOR CH-66 × 2	Consistent with protein count
9	Protein heterocomplex	Heteromer	Protein 2	INHIBITOR CH-66 × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RENS_MOUSE
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–335； UniProt 67–401 Author chain C； PDBConstruct 1–335； UniProt 67–401 Author chain E； PDBConstruct 1–335； UniProt 67–401 Author chain G； PDBConstruct 1–335； UniProt 67–401

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	1smr
Deposition date deposition_date	1992-03-11
Structure title title	The 3-d structure of mouse submaxillary renin complexed with a decapeptide inhibitor ch-66 based on the 4-16 fragment of rat angiotensinogen
Keywords keywords	ASPARTIC PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

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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.

1smr__assembly_9__model_1

Assembly 9 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1smr__assembly_9__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1smr__assembly_9__model_1 | P(r) · Pending

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

Rg（Guinier）	20.79 Å
Rg (electron density)	19.48 Å
Total Rg	20.59 Å
Atom count	2601
Residues	338
Excluded volume	46496 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1smr__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1smr__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1smr__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`1smr__assembly_4__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
5	1	`1smr__assembly_5__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
6	1	`1smr__assembly_6__model_1`	octameric （8）	Success	4.1.3-1-20251215 (887e7ef)	View Download
7	1	`1smr__assembly_7__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
8	1	`1smr__assembly_8__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
9	1	`1smr__assembly_9__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
10	1	`1smr__assembly_10__model_1`	tetrameric （4）	Success	4.1.3-1-20251215 (887e7ef)	View Download
11	1	`1smr__assembly_11__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
12	1	`1smr__assembly_12__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
13	1	`1smr__assembly_13__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	RENIN
Molecular weight formula_weight	36533.3 kDa
EC 编号 ec_number	3.4.23.15
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G
Atom count atom_count	10560

TDLISPVVLTNYLNSQYYGEIGIGTPPQTFKVIFDTGSANLWVPSTKCSRLYLACGIHSLYESSDSSSYMENGDDFTIHYGSGRVKGFLSQDSVTVGGITVTQTFGEVTQLPLIPFMLAQFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEKVFSVYYNRGPHLLGGEVVLGGSDPQHYQGDFHYVSLSKTDSWQITMKGVSVGSSTLLCEEGCEVVVDTGSSFISAPTSSLKLIMQALGAKEKRLHEYVVSCSQVPTLPDISFNLGGRAYTLSSTDYVLQYPNRRDKLCTVALHAMDIPPPTGPVWVLGATFIRKFYTEFDRHNNRIGFALAR

Source Source

Source organism organism	Mus musculus
Common name common_name	house mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090

Entity 2 Entity 2 polymer

Description description	INHIBITOR CH-66
Molecular weight formula_weight	1263.5 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

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

XHPFHXYYS

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	156

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6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1smra_
Class class	b — All beta proteins
Fold Fold fold	b.50 — Acid proteases
Superfamily Superfamily superfamily	b.50.1 — Acid proteases
Family Family family	b.50.1.2 — Pepsin-like

Domain ID domain_id	d1smrc_
Class class	b — All beta proteins
Fold Fold fold	b.50 — Acid proteases
Superfamily Superfamily superfamily	b.50.1 — Acid proteases
Family Family family	b.50.1.2 — Pepsin-like

Domain ID domain_id	d1smre_
Class class	b — All beta proteins
Fold Fold fold	b.50 — Acid proteases
Superfamily Superfamily superfamily	b.50.1 — Acid proteases
Family Family family	b.50.1.2 — Pepsin-like

Domain ID domain_id	d1smrg_
Class class	b — All beta proteins
Fold Fold fold	b.50 — Acid proteases
Superfamily Superfamily superfamily	b.50.1 — Acid proteases
Family Family family	b.50.1.2 — Pepsin-like

CATH v4.4 (8 domains)

Domain ID domain_id	1smrA01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acid Proteases

Domain ID domain_id	1smrA02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acid Proteases

Domain ID domain_id	1smrC01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acid Proteases

Domain ID domain_id	1smrC02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acid Proteases

Domain ID domain_id	1smrE01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acid Proteases

Domain ID domain_id	1smrE02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acid Proteases

Domain ID domain_id	1smrG01
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acid Proteases

Domain ID domain_id	1smrG02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily	10 — Acid Proteases

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Unit-cell length a length_a	78.340 Å
Unit-cell length b length_b	117.760 Å
Unit-cell length c length_c	85.880 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	101.18 °
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	2.000 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	0.1800
R_work r_work	—
R_free r_free	—

The 3-d structure of mouse submaxillary renin complexed with a decapeptide inhibitor ch-66 based on the 4-16 fragment of rat angiotensinogen

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

RENIN

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

1smr__assembly_9__model_1

1smr__assembly_9__model_1 | I(q)

1smr__assembly_9__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (3)

The 3-d structure of mouse submaxillary renin complexed with a decapeptide inhibitor ch-66 based on the 4-16 fragment of rat angiotensinogen

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

RENIN

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

1smr__assembly_9__model_1

1smr__assembly_9__model_1 | I(q)

1smr__assembly_9__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (4 domains)

CATH v4.4 (8 domains)

7. Citations (3)