1wos

Crystal Structure of T-protein of the Glycine Cleavage System

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

Aminomethyltransferase

Thermotoga maritima

UniProt Q9WY54

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 GCST_THEMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–364; UniProt 1–364

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_id1wos
Deposition date deposition_date2004-08-24
Structure title titleCrystal Structure of T-protein of the Glycine Cleavage System
Keywords keywordsaminomethyltransferase, T-protein, 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.

1wos__assembly_1__model_1

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

Download this curve (.dat)

1wos__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.

1wos__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)21.56 Å
Rg (electron density)20.50 Å
Total Rg21.46 Å
Atom count2810
Residues361
Excluded volume50614 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1wos__assembly_1__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 (2)

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1wosa1
Class classb — All beta proteins
Fold Fold foldb.44 — Elongation factor/aminomethyltransferase common domain
Superfamily Superfamily superfamilyb.44.2 — Aminomethyltransferase beta-barrel domain
Family Family familyb.44.2.1 — Aminomethyltransferase beta-barrel domain
Domain ID domain_idd1wosa2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.250 — Folate-binding domain
Superfamily Superfamily superfamilyd.250.1 — Folate-binding domain
Family Family familyd.250.1.1 — Aminomethyltransferase folate-binding domain

CATH v4.4 (4 domains)

Domain ID domain_id1wosA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1360 — Gyrase A; domain 2
Homologous superfamily homologous superfamily120 — Probable tRNA modification gtpase trme; domain 1
Domain ID domain_id1wosA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1400 — Aminomethyltransferase beta-barrel domains
Domain ID domain_id1wosA03
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology1250 — Aminomethyltransferase fragment
Homologous superfamily homologous superfamily10 — Aminomethyltransferase fragment
Domain ID domain_id1wosA04
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily110 — Aminomethyltransferase beta-barrel domains
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7. Citations (1)