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1ebw

HIV-1 protease in complex with the inhibitor BEA322

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

HIV-1 PROTEASE

Human immunodeficiency virus 1

UniProt P03366

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 N,N-[2,5-O-[DIBENZYL]-GLUCARYL]-DI-[ISOLEUCYL-AMIDO-METHANE] × 1 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1rdh 1rdh 3k2p 3k2p 4qag 4qag

6 assemblies

Homodimer
1ajv 1ajx 1axa 1bqm 1bqn 1d4h 1d4i 1d4j 1dlo 1dw6 1ebk 1ebk

289 assemblies; showing the first 12

Homotetramer
1eet 1ikv 1ikw 1ikx 1iky 9mxt

6 assemblies

Other homooligomers
7snl 7snn

2 assemblies

Heteromeric or nucleic-acid complex
1hef 1hni 1hte 1hvu 1hvu 1hvu 1hvu 1hys 1j5o 1n5y 1n6q 1r0a

167 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name POL_HV1B1
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–99； UniProt 69–167 Author chain B； PDBConstruct 1–99； UniProt 69–167

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_id1ebw
Deposition date deposition_date2000-01-25
Structure title titleHIV-1 protease in complex with the inhibitor BEA322
Keywords keywordsDimer, protein-inhibitor complex, 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.

1ebw__assembly_1__model_1

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

Download this curve (.dat)

1ebw__assembly_1__model_1 | I(q)

10-2 10-1 105 106 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1ebw__assembly_1__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）18.16 Å
Rg (electron density)17.20 Å
Total Rg18.20 Å
Atom count1556
Residues198
Excluded volume28469 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1ebw__assembly_1__model_1 dimeric （2） 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)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ebwa_
Class classb — All beta proteins
Fold Fold foldb.50 — Acid proteases
Superfamily Superfamily superfamilyb.50.1 — Acid proteases
Family Family familyb.50.1.1 — Retroviral protease (retropepsin)
Domain ID domain_idd1ebwb_
Class classb — All beta proteins
Fold Fold foldb.50 — Acid proteases
Superfamily Superfamily superfamilyb.50.1 — Acid proteases
Family Family familyb.50.1.1 — Retroviral protease (retropepsin)

CATH v4.4 (2 domains)

Domain ID domain_id1ebwA00
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_id1ebwB00
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)