1dg3

STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM

Method: X-RAY DIFFRACTION

1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (INTERFERON-INDUCED GUANYLATE-BINDING PROTEIN 1)

Homo sapiens

UniProt P32455

State in the Current Structure

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

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name GBP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–592; UniProt 1–592

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1dg3
Deposition date deposition_date1999-11-23
Structure title titleSTRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM
Keywords keywordsGBP, GTP HYDROLYSIS, GDP, GMP, INTERFERON INDUCED, DYNAMIN RELATED, LARGE GTPASE FAMILY, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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.

1dg3__assembly_1__model_1

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

Download this curve (.dat)

1dg3__assembly_1__model_1 | I(q)

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

1dg3__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)37.77 Å
Rg (electron density)38.95 Å
Total Rg38.79 Å
Atom count4357
Residues540
Excluded volume77957 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1dg3__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (2)

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1dg3a1
Class classa — All alpha proteins
Fold Fold folda.114 — Interferon-induced guanylate-binding protein 1 (GBP1), C-terminal domain
Superfamily Superfamily superfamilya.114.1 — Interferon-induced guanylate-binding protein 1 (GBP1), C-terminal domain
Family Family familya.114.1.1 — Interferon-induced guanylate-binding protein 1 (GBP1), C-terminal domain
Domain ID domain_idd1dg3a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (2 domains)

Domain ID domain_id1dg3A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1000 — Signaling Protein - Interferon-induced Guanylate-binding Protein 1; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Guanylate-binding protein, C-terminal domain
Domain ID domain_id1dg3A02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

7. Citations (2)