3mhp

FNR-recruitment to the thylakoid

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

Ferredoxin--NADP reductase, leaf isozyme, chloroplastic

Pisum sativum

UniProt P10933

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 TIC62_peptide × 1 (Q8SKU2) FLAVIN-ADENINE DINUCLEOTIDE × 2 water × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FENR1_PEA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–295; UniProt 66–360 Author chain B; PDBConstruct 1–295; UniProt 66–360

TIC62_peptide

OrganismNot specified

UniProt Q8SKU2

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 3 Ferredoxin--NADP reductase, leaf isozyme, chloroplastic × 2 (P10933) FLAVIN-ADENINE DINUCLEOTIDE × 2 water × 3 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q8SKU2_PEA
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–26; UniProt 383–408

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_id3mhp
Deposition date deposition_date2010-04-08
Structure title titleFNR-recruitment to the thylakoid
Keywords keywordsFNR, oxidoreductase, thylakoid membrane, proton-flux, poly proline II helix, self assembly, NADP(H); 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.

3mhp__assembly_1__model_1

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

Download this curve (.dat)

3mhp__assembly_1__model_1 | I(q)

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

3mhp__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)28.45 Å
Rg (electron density)27.80 Å
Total Rg28.54 Å
Atom count4967
Residues611
Excluded volume88942 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3mhp__assembly_1__model_1 trimeric (3) 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 (4)

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6. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id3mhpA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id3mhpA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily80 — Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module
Domain ID domain_id3mhpB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology30 — Elongation Factor Tu (Ef-tu); domain 3
Homologous superfamily homologous superfamily10 — Translation factors
Domain ID domain_id3mhpB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily80 — Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module
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7. Citations (1)