5c7m

CRYSTAL STRUCTURE OF E3 LIGASE ITCH WITH A UB VARIANT

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

E3 ubiquitin-protein ligase Itchy homolog

Homo sapiens

UniProt Q96J02

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Polyubiquitin-C × 1 (P0CG48) water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ITCH_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 19–394; UniProt 524–899

Polyubiquitin-C

Homo sapiens

UniProt P0CG48

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 E3 ubiquitin-protein ligase Itchy homolog × 1 (Q96J02) water × 1 Consistent with protein count
2 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–75; UniProt 1–75 Author chain C; PDBConstruct 1–75; UniProt 1–75

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_id5c7m
Deposition date deposition_date2015-06-24
Structure title titleCRYSTAL STRUCTURE OF E3 LIGASE ITCH WITH A UB VARIANT
Keywords keywords;LIGASE, UBIQUITIN-PROTEIN LIGASE, UBIQUITIN VARIANT, Structural Genomics Consortium, SGC, Structural Genomics, LIGASE-SIGNALING PROTEIN complex ;; LIGASE/SIGNALING PROTEIN
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.

5c7m__assembly_1__model_1

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

Download this curve (.dat)

5c7m__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

5c7m__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)25.35 Å
Rg (electron density)24.29 Å
Total Rg25.12 Å
Atom count3294
Residues441
Excluded volume57603 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5c7m__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 5c7m__assembly_2__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)

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd5c7ma_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.148 — Hect, E3 ligase catalytic domain
Superfamily Superfamily superfamilyd.148.1 — Hect, E3 ligase catalytic domain
Family Family familyd.148.1.0 — automated matches
Domain ID domain_idd5c7mb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
Domain ID domain_idd5c7mc_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related
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7. Citations (1)