2kbo

Structure, interaction, and real-time monitoring of the enzymatic reaction of wild type APOBEC3G

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

DNA dC->dU-editing enzyme APOBEC-3G

Homo sapiens

UniProt Q9HC16

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 ZINC ION × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ABC3G_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–194; UniProt 193–384

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_id2kbo
Deposition date deposition_date2008-12-04
Structure title titleStructure, interaction, and real-time monitoring of the enzymatic reaction of wild type APOBEC3G
Keywords keywords;Cytidine deaminase, HIV, APOBEC3G, Alternative splicing, Antiviral defense, Cytoplasm, Host-virus interaction, Hydrolase, Metal-binding, Nucleus, Polymorphism, Ubl conjugation, Zinc ;; HYDROLASE
Experimental Method methodSOLUTION NMR
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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.

2kbo__assembly_1__model_3

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

Download this curve (.dat)

2kbo__assembly_1__model_3 | I(q)

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

2kbo__assembly_1__model_3 | 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)19.40 Å
Rg (electron density)18.11 Å
Total Rg18.99 Å
Atom count3128
Residues194
Excluded volume28208 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2kbo__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 2kbo__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 2kbo__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 2kbo__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 2kbo__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 2kbo__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 2kbo__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 2kbo__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 2kbo__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 2kbo__assembly_1__model_10 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 (2)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2kboa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.97 — Cytidine deaminase-like
Superfamily Superfamily superfamilyc.97.1 — Cytidine deaminase-like
Family Family familyc.97.1.6 — apolipoprotein B messenger RNA-editing enzyme catalytic (APOBEC) cytidine deaminase domains
Domain ID domain_idd2kboa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
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7. Citations (1)