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3own

Potent macrocyclic renin inhibitors

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Renin

OrganismNot specified

UniProt P00797

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 ACETATE ION × 3 SODIUM ION × 2 ;(2S,4S)-4-hydroxy-2-(1-methylethyl)-4-[(4R,13S)-18-[methyl(methylsulfonyl)amino]-2,15-dioxo-4-phenyl-11-oxa-3,14-diazatricyclo[14.3.1.1~5,9~]henicosa-1(20),5(21),6,8,16,18-hexaen-13-yl]-N-(2-methylpropyl)butanamide ; × 1 water × 1 Consistent with protein count
2 Protein monomer Monomer Protein 1 ;(2S,4S)-4-hydroxy-2-(1-methylethyl)-4-[(4S,13S)-18-[methyl(methylsulfonyl)amino]-2,15-dioxo-4-phenyl-11-oxa-3,14-diazatricyclo[14.3.1.1~5,9~]henicosa-1(20),5(21),6,8,16,18-hexaen-13-yl]-N-(2-methylpropyl)butanamide ; × 1 water × 1 Consistent with protein count
3 Protein homooligomer Homooligomer Protein 3 ACETATE ION × 9 SODIUM ION × 6 ;(2S,4S)-4-hydroxy-2-(1-methylethyl)-4-[(4R,13S)-18-[methyl(methylsulfonyl)amino]-2,15-dioxo-4-phenyl-11-oxa-3,14-diazatricyclo[14.3.1.1~5,9~]henicosa-1(20),5(21),6,8,16,18-hexaen-13-yl]-N-(2-methylpropyl)butanamide ; × 3 water × 3 Consistent with protein count
4 Protein homooligomer Homooligomer Protein 3 ;(2S,4S)-4-hydroxy-2-(1-methylethyl)-4-[(4S,13S)-18-[methyl(methylsulfonyl)amino]-2,15-dioxo-4-phenyl-11-oxa-3,14-diazatricyclo[14.3.1.1~5,9~]henicosa-1(20),5(21),6,8,16,18-hexaen-13-yl]-N-(2-methylpropyl)butanamide ; × 3 water × 3 Consistent with protein count
5 Protein homooligomer Homooligomer Protein 6 ACETATE ION × 9 SODIUM ION × 6 ;(2S,4S)-4-hydroxy-2-(1-methylethyl)-4-[(4R,13S)-18-[methyl(methylsulfonyl)amino]-2,15-dioxo-4-phenyl-11-oxa-3,14-diazatricyclo[14.3.1.1~5,9~]henicosa-1(20),5(21),6,8,16,18-hexaen-13-yl]-N-(2-methylpropyl)butanamide ; × 3 ;(2S,4S)-4-hydroxy-2-(1-methylethyl)-4-[(4S,13S)-18-[methyl(methylsulfonyl)amino]-2,15-dioxo-4-phenyl-11-oxa-3,14-diazatricyclo[14.3.1.1~5,9~]henicosa-1(20),5(21),6,8,16,18-hexaen-13-yl]-N-(2-methylpropyl)butanamide ; × 3 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1bbs 1bbs 2bks 2bks 2bkt 2bkt 2fs4 2fs4 2g1n 2g1n 2g1o 2g1o

139 assemblies; showing the first 12

Homodimer
1bil 1bim 1hrn 1rne 2i4q 2v12 2v12 3d91 3g6z 3g70 3g72 3k1w

21 assemblies; showing the first 12

Homotetramer

None

Other homooligomers
1bbs 1bbs 2fs4 2fs4 2fs4 2g1o 2g1o 2g1o 2g1r 2g1y 2g1y 2g1y

57 assemblies; showing the first 12

Heteromeric or nucleic-acid complex
2x0b 2x0b 2x0b 2x0b 3gw5 3km4 3q3t 3q5h 4amt 5sxn 5sxn 5sy3

13 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name RENI_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–340； UniProt 67–406 Author chain B； PDBConstruct 1–340； UniProt 67–406

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_id3own
Deposition date deposition_date2010-09-20
Structure title titlePotent macrocyclic renin inhibitors
Keywords keywordsRENIN, PROTEASE, ASPARTYL PROTEASE, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-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.

3own__assembly_3__model_1

Assembly 3 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3own__assembly_3__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

3own__assembly_3__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg（Guinier）31.76 Å
Rg (electron density)30.46 Å
Total Rg31.13 Å
Atom count7909
Residues1002
Excluded volume141330 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3own__assembly_1__model_1 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 3own__assembly_2__model_1 monomeric （1） Success 4.1.3-1-20251215 (887e7ef) View Download
3 1 3own__assembly_3__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
4 1 3own__assembly_4__model_1 trimeric （3） Success 4.1.3-1-20251215 (887e7ef) View Download
5 1 3own__assembly_5__model_1 hexameric （6） 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 (6)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3owna_
Class classb — All beta proteins
Fold Fold foldb.50 — Acid proteases
Superfamily Superfamily superfamilyb.50.1 — Acid proteases
Family Family familyb.50.1.2 — Pepsin-like
Domain ID domain_idd3ownb_
Class classb — All beta proteins
Fold Fold foldb.50 — Acid proteases
Superfamily Superfamily superfamilyb.50.1 — Acid proteases
Family Family familyb.50.1.2 — Pepsin-like

CATH v4.4 (4 domains)

Domain ID domain_id3ownA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily10 — Acid Proteases
Domain ID domain_id3ownA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily10 — Acid Proteases
Domain ID domain_id3ownB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily10 — Acid Proteases
Domain ID domain_id3ownB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology70 — Cathepsin D, subunit A; domain 1
Homologous superfamily homologous superfamily10 — Acid Proteases
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7. Citations (1)