1y6h

Crystal structure of LIPDF

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

Peptide deformylase

Leptospira interrogans

UniProt Q93LE9

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 ZINC ION × 2 FORMIC ACID × 8 GLYCINE × 1 water × 2 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 4 ZINC ION × 4 FORMIC ACID × 16 GLYCINE × 2 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DEF_LEPIN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–177; UniProt 2–178 Author chain B; PDBConstruct 1–177; UniProt 2–178

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_id1y6h
Deposition date deposition_date2004-12-06
Structure title titleCrystal structure of LIPDF
Keywords keywordsopen and close conformation, PDF, HYDROLASE; HYDROLASE
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.

1y6h__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1y6h__assembly_2__model_1 | I(q)

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

1y6h__assembly_2__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)31.04 Å
Rg (electron density)30.40 Å
Total Rg31.00 Å
Atom count5668
Residues708
Excluded volume100860 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1y6h__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1y6h__assembly_2__model_1 tetrameric (4) 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 (5)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1y6ha_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.167 — Peptide deformylase
Superfamily Superfamily superfamilyd.167.1 — Peptide deformylase
Family Family familyd.167.1.1 — Peptide deformylase
Domain ID domain_idd1y6hb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.167 — Peptide deformylase
Superfamily Superfamily superfamilyd.167.1 — Peptide deformylase
Family Family familyd.167.1.1 — Peptide deformylase

CATH v4.4 (2 domains)

Domain ID domain_id1y6hA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology45 — Peptide Deformylase
Homologous superfamily homologous superfamily10 — Peptide deformylase
Domain ID domain_id1y6hB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology45 — Peptide Deformylase
Homologous superfamily homologous superfamily10 — Peptide deformylase
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7. Citations (1)