1dmr

OXIDIZED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS

Method: X-RAY DIFFRACTION

1. Protein Identity and Related Structures Protein Identity & Related Structures

DMSO REDUCTASE

OrganismNot specified

UniProt Q52675

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE × 2 MOLYBDENUM(VI) ION × 1 OXYGEN ATOM × 2 water × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name DMSA_RHOCA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–823; UniProt 1–823

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1dmr
Deposition date deposition_date1997-04-22
Structure title titleOXIDIZED DMSO REDUCTASE FROM RHODOBACTER CAPSULATUS
Keywords keywordsOXIDOREDUCTASE, REDUCTASE, DMSO, MOLYBDOPTERIN; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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.

1dmr__assembly_1__model_1

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

Download this curve (.dat)

1dmr__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.

1dmr__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)26.67 Å
Rg (electron density)25.83 Å
Total Rg26.71 Å
Atom count6069
Residues779
Excluded volume107080 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1dmr__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (5)

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1dmra1
Class classb — All beta proteins
Fold Fold foldb.52 — Double psi beta-barrel
Superfamily Superfamily superfamilyb.52.2 — ADC-like
Family Family familyb.52.2.2 — Formate dehydrogenase/DMSO reductase, C-terminal domain
Domain ID domain_idd1dmra2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.81 — Formate dehydrogenase/DMSO reductase, domains 1-3
Superfamily Superfamily superfamilyc.81.1 — Formate dehydrogenase/DMSO reductase, domains 1-3
Family Family familyc.81.1.1 — Formate dehydrogenase/DMSO reductase, domains 1-3

CATH v4.4 (4 domains)

Domain ID domain_id1dmrA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily740
Domain ID domain_id1dmrA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology228 — Dimethylsulfoxide Reductase; domain 2
Homologous superfamily homologous superfamily10 — Dimethylsulfoxide Reductase, domain 2
Domain ID domain_id1dmrA03
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology55 — Dimethylsulfoxide Reductase; domain 3
Homologous superfamily homologous superfamily10 — Dimethylsulfoxide Reductase, domain 3
Domain ID domain_id1dmrA04
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology40 — Barwin-like endoglucanases
Homologous superfamily homologous superfamily20

7. Citations (1)