1s96

The 2.0 A X-ray structure of Guanylate Kinase from E.coli

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

Guanylate kinase

Escherichia coli

UniProt P60546

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 PHOSPHATE ION × 2 UNKNOWN ATOM OR ION × 1 water × 2 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 6 PHOSPHATE ION × 6 UNKNOWN ATOM OR ION × 3 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name KGUA_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 13–219; UniProt 1–207 Author chain B; PDBConstruct 13–219; UniProt 1–207

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_id1s96
Deposition date deposition_date2004-02-03
Structure title titleThe 2.0 A X-ray structure of Guanylate Kinase from E.coli
Keywords keywordsguanylate kinase, E.coli, dimer, SAD, transferase; TRANSFERASE
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.

Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1s96__assembly_1__model_1 dimeric (2) Excluded — —
Exclusion reason: The source record does not identify the atom or ion element unambiguously, so a reliable calculation is not possible.
2 1 1s96__assembly_2__model_1 hexameric (6) Excluded — —
Exclusion reason: The source record does not identify the atom or ion element unambiguously, so a reliable calculation is not possible.
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1s96a_
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.37.1.1 — Nucleotide and nucleoside kinases
Domain ID domain_idd1s96b_
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.37.1.1 — Nucleotide and nucleoside kinases

CATH v4.4 (4 domains)

Domain ID domain_id1s96A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1s96A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology63 — Guanylate Kinase phosphate binding domain
Homologous superfamily homologous superfamily10 — Guanylate Kinase phosphate binding domain
Domain ID domain_id1s96B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id1s96B02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology63 — Guanylate Kinase phosphate binding domain
Homologous superfamily homologous superfamily10 — Guanylate Kinase phosphate binding domain
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7. Citations (1)