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1p04

STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES

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

ALPHA-LYTIC PROTEASE

Lysobacter enzymogenes

UniProt P00778

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 METHOXYSUCCINYL-ALA-ALA-PRO-ISOLEUCINE BORONIC ACID INHIBITOR × 1 SULFATE ION × 1 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

Monomer
1boq 1gba 1gbe 1gbj 1p01 1p09 1qq4 1qrw 1qrx 1ssx 1tal 2alp

23 assemblies; showing the first 12

Homodimer
3pro 3pro 4pro 4pro

4 assemblies

Homotetramer

None

Other homooligomers
2pro

1 assemblies

Heteromeric or nucleic-acid complex
1gbb 1gbc 1gbd 1gbf 1gbh 1gbi 1gbk 1gbl 1gbm 1p02 1p03 1p04

29 assemblies; showing the first 12

View Construct and Data Evidence
UniProt name PRLA_LYSEN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–198； UniProt 200–397

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_id1p04
Deposition date deposition_date1989-04-24
Structure title titleSTRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES
Keywords keywordsHYDROLASE-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.

1p04__assembly_1__model_1

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

Download this curve (.dat)

1p04__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.

1p04__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）16.20 Å
Rg (electron density)15.03 Å
Total Rg16.11 Å
Atom count1422
Residues201
Excluded volume24880 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1p04__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 (4)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1p04a_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.1 — Prokaryotic proteases

CATH v4.4 (2 domains)

Domain ID domain_id1p04A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1p04A02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
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7. Citations (6)