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1feb

UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.0 ANGSTROM RESOLUTION

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

TRYPANOTHIONE REDUCTASE

Crithidia fasciculata

UniProt P39040

State in the Current Structure

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

Other States of the Same Protein in the Database

Monomer

None

Homodimer
1fea 1fea 1feb 1fec 1typ 1tyt 2tpr

7 assemblies

Homotetramer

None

Other homooligomers

None

Heteromeric or nucleic-acid complex

None

View Construct and Data Evidence
UniProt name TYTR_CRIFA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–490； UniProt 2–491 Author chain B； PDBConstruct 1–490； UniProt 2–491

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_id1feb
Deposition date deposition_date1995-07-12
Structure title titleUNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.0 ANGSTROM RESOLUTION
Keywords keywordsREDOX-ACTIVE CENTER, OXIDOREDUCTASE, FLAVOPROTEIN, FAD, NADP; OXIDOREDUCTASE
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.

1feb__assembly_1__model_1

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

Download this curve (.dat)

1feb__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.

1feb__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）31.76 Å
Rg (electron density)30.95 Å
Total Rg31.40 Å
Atom count7501
Residues971
Excluded volume132610 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1feb__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) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1feba1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains
Domain ID domain_idd1feba2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains
Domain ID domain_idd1feba3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.87 — CO dehydrogenase flavoprotein C-domain-like
Superfamily Superfamily superfamilyd.87.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain
Family Family familyd.87.1.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain
Domain ID domain_idd1febb1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains
Domain ID domain_idd1febb2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamilyc.3.1 — FAD/NAD(P)-binding domain
Family Family familyc.3.1.5 — FAD/NAD-linked reductases, N-terminal and central domains
Domain ID domain_idd1febb3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.87 — CO dehydrogenase flavoprotein C-domain-like
Superfamily Superfamily superfamilyd.87.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain
Family Family familyd.87.1.1 — FAD/NAD-linked reductases, dimerisation (C-terminal) domain

CATH v4.4 (6 domains)

Domain ID domain_id1febA01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1febA02
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1febA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily30 — FAD/NAD-linked reductase, C-terminal dimerisation domain
Domain ID domain_id1febB01
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1febB02
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily60 — FAD/NAD(P)-binding domain
Domain ID domain_id1febB03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology390 — Enolase-like; domain 1
Homologous superfamily homologous superfamily30 — FAD/NAD-linked reductase, C-terminal dimerisation domain
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7. Citations (6)