2mj3

Backbone 1H, 13C, and 15N Chemical Shift Assignments and structure of Iron-sulfur cluster binding protein from Ehrlichia chaffeensis

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Iron-sulfur cluster binding protein

Ehrlichia chaffeensis

UniProt Q2GGI9

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q2GGI9_EHRCR
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–116; UniProt 1–116

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_id2mj3
Deposition date deposition_date2013-12-23
Structure title titleBackbone 1H, 13C, and 15N Chemical Shift Assignments and structure of Iron-sulfur cluster binding protein from Ehrlichia chaffeensis
Keywords keywords;Ehrlichia chaffeensis, Iron-sulfur cluster binding protein, METAL BINDING PROTEIN, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID ;; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR
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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.

2mj3__assembly_1__model_9

Assembly 1 · Model 9 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

2mj3__assembly_1__model_9 | I(q)

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

2mj3__assembly_1__model_9 | 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)16.41 Å
Rg (electron density)14.99 Å
Total Rg16.03 Å
Atom count1764
Residues116
Excluded volume15859 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2mj3__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 2mj3__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 2mj3__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 2mj3__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 2mj3__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 2mj3__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 2mj3__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 2mj3__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 2mj3__assembly_1__model_9 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 (1)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2mj3a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.4 — 2Fe-2S ferredoxin-like
Family Family familyd.15.4.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id2mj3A00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily30 — Beta-grasp domain
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7. Citations (1)