1vly

Crystal structure of a putative aminomethyltransferase (ygfz) from escherichia coli at 1.30 A resolution

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

Unknown protein from 2D-page

Escherichia coli

UniProt P39179

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 ACETATE ION × 1 CALCIUM ION × 1 CHLORIDE ION × 1 1,2-ETHANEDIOL × 3 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name UP14_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–338; UniProt 1–325

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_id1vly
Deposition date deposition_date2004-08-20
Structure title titleCrystal structure of a putative aminomethyltransferase (ygfz) from escherichia coli at 1.30 A resolution
Keywords keywordsStructural genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI, 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.

1vly__assembly_1__model_1

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

Download this curve (.dat)

1vly__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.

1vly__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)20.80 Å
Rg (electron density)19.69 Å
Total Rg20.65 Å
Atom count2493
Residues314
Excluded volume44524 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1vly__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 (6)

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6. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1vlya1
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_idd1vlya2
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 (3 domains)

Domain ID domain_id1vlyA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily1630 —
Domain ID domain_id1vlyA02
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_id1vlyA03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily160 —
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7. Citations (1)