1bg0

TRANSITION STATE STRUCTURE OF ARGININE KINASE

Method: X-RAY DIFFRACTION
▼

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

ARGININE KINASE

Limulus polyphemus

UniProt P51541

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 NITRATE ION × 2 MAGNESIUM ION × 1 ADENOSINE-5'-DIPHOSPHATE × 1 D-ARGININE × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name KARG_LIMPO
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–356; UniProt 2–357

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_id1bg0
Deposition date deposition_date1998-06-03
Structure title titleTRANSITION STATE STRUCTURE OF ARGININE KINASE
Keywords keywordsARGININE KINASE, CREATINE KINASE, PHOSPHAGEN KINASE, TRANSITION STATE ANALOG, ADENOSINE TRIPHOSPHATE, TRANSFERASE, KINASE; KINASE
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.

1bg0__assembly_1__model_1

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

Download this curve (.dat)

1bg0__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.

1bg0__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)20.68 Å
Rg (electron density)19.98 Å
Total Rg20.92 Å
Atom count2865
Residues356
Excluded volume50736 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1bg0__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 (6)

▼

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1bg0a1
Class classa — All alpha proteins
Fold Fold folda.83 — Guanido kinase N-terminal domain
Superfamily Superfamily superfamilya.83.1 — Guanido kinase N-terminal domain
Family Family familya.83.1.1 — Guanido kinase N-terminal domain
Domain ID domain_idd1bg0a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.128 — Glutamine synthetase/guanido kinase
Superfamily Superfamily superfamilyd.128.1 — Glutamine synthetase/guanido kinase
Family Family familyd.128.1.2 — Guanido kinase catalytic domain

CATH v4.4 (2 domains)

Domain ID domain_id1bg0A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology135 — Transferase Creatine Kinase; Chain A, domain 1
Homologous superfamily homologous superfamily10 — ATP:guanido phosphotransferase, N-terminal domain
Domain ID domain_id1bg0A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology590 — Creatine Kinase; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Glutamine synthetase/guanido kinase, catalytic domain
▶

7. Citations (3)