1vjt

Crystal structure of Alpha-glucosidase (TM0752) from Thermotoga maritima at 2.50 A resolution

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

alpha-glucosidase

Thermotoga maritima

UniProt Q9WZL1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q9WZL1_THEMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 13–483; UniProt 1–471

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_id1vjt
Deposition date deposition_date2004-03-22
Structure title titleCrystal structure of Alpha-glucosidase (TM0752) from Thermotoga maritima at 2.50 A resolution
Keywords keywords;TM0752, ALPHA-GLUCOSIDASE, STRUCTURAL GENOMICS, JCSG, PSI, Protein Structure Initiative, Joint Center for Structural Genomics, HYDROLASE ;; HYDROLASE
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.

1vjt__assembly_1__model_1

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

Download this curve (.dat)

1vjt__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1vjt__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)32.78 Å
Rg (electron density)32.21 Å
Total Rg32.82 Å
Atom count7816
Residues912
Excluded volume139250 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1vjt__assembly_1__model_1 dimeric (2) 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 (3)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1vjta1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.5 — LDH N-terminal domain-like
Domain ID domain_idd1vjta2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.162 — LDH C-terminal domain-like
Superfamily Superfamily superfamilyd.162.1 — LDH C-terminal domain-like
Family Family familyd.162.1.2 — AglA-like glucosidase
Domain ID domain_idd1vjta3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1vjtA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
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7. Citations (1)