1naa

Cellobiose Dehydrogenase Flavoprotein Fragment in Complex with Cellobionolactam

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

Cellobiose dehydrogenase

OrganismNot specified

UniProt Q01738

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE × 1 (2R,3R,4R,5R)-4,5-dihydroxy-2-(hydroxymethyl)-6-oxopiperidin-3-yl beta-D-glucopyranoside × 1 water × 1 Consistent with protein count
2 Protein monomer Monomer Protein 1 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 6-HYDROXY-FLAVIN-ADENINE DINUCLEOTIDE × 1 (2R,3R,4R,5R)-4,5-dihydroxy-2-(hydroxymethyl)-6-oxopiperidin-3-yl beta-D-glucopyranoside × 1 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CDH_PHACH
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–541; UniProt 233–773 Author chain B; PDBConstruct 1–541; UniProt 233–773

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_id1naa
Deposition date deposition_date2002-11-27
Structure title titleCellobiose Dehydrogenase Flavoprotein Fragment in Complex with Cellobionolactam
Keywords keywordsGMC oxidoreductase, alpha/beta structure, rossmann fold, PHBH fold, product analogue complex, 6-hydroxylated FAD, OXIDOREDUCTASE; 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.

1naa__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1naa__assembly_2__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1naa__assembly_2__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)23.66 Å
Rg (electron density)22.75 Å
Total Rg23.65 Å
Atom count4172
Residues541
Excluded volume73638 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1naa__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1naa__assembly_2__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 (5)

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6. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1naaa1
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.3.1.2 — FAD-linked reductases, N-terminal domain
Domain ID domain_idd1naaa2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamilyd.16.1 — FAD-linked reductases, C-terminal domain
Family Family familyd.16.1.1 — GMC oxidoreductases
Domain ID domain_idd1naab1
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.3.1.2 — FAD-linked reductases, N-terminal domain
Domain ID domain_idd1naab2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamilyd.16.1 — FAD-linked reductases, C-terminal domain
Family Family familyd.16.1.1 — GMC oxidoreductases

CATH v4.4 (4 domains)

Domain ID domain_id1naaA01
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_id1naaA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology410 — Cholesterol Oxidase; domain 2
Homologous superfamily homologous superfamily10 — Cholesterol Oxidase; domain 2
Domain ID domain_id1naaB01
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_id1naaB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology410 — Cholesterol Oxidase; domain 2
Homologous superfamily homologous superfamily10 — Cholesterol Oxidase; domain 2
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7. Citations (2)