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1b9r

TERPREDOXIN FROM PSEUDOMONAS SP.

Method: SOLUTION NMR Dmax: 39.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (TERPREDOXIN)

Pseudomonas sp.

UniProt P33007

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–105 Not recorded FES FE2/S2 (INORGANIC) CLUSTER × 1 SOLUTION NMR NMR measurement conditions：pH 7.4；290 K；Pressure 1 Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1B9R Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9Q36 Crystal structure of C43S terpredoxin, a [2Fe-2S] ferredoxin from Pseudomonas sp Deposited 2025-08-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–106（105 aa）
Chain B 2–106（105 aa）
Mutation：C44S Mutation：C44S FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；1.6 M sodium citrate pH 6.5
Resolution 2.10 Å R-free 0.271

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TERPB_PSESP
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–105； UniProt 1–105

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.

SAXS scattering curve SAXS Profile

SAXS profile for 1b9r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b9r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b9r
Deposition date deposition_date1999-02-15
Structure title titleTERPREDOXIN FROM PSEUDOMONAS SP.
Keywords keywordsSTRUCTURE FROM MOLMOL, FERREDOXIN; FERREDOXIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.91 Å
Radius of gyration Rg (electron density) rg_electron12.57 Å
Forward intensity I(0) i0464796000.00
Molecular weight molecular_weight168890.0 kDa
Excluded volume excluded_volume205440 ų
Envelope volume envelope_volume20536 ų
Hydration-shell volume shell_volume12601 ų
Envelope diameter envelope_diameter45.1 Å
Shell Rg shell_rg19.66 Å
Envelope Rg envelope_rg13.96 Å
Shape Rg shape_rg12.61 Å
Total Rg total_rg12.59 Å
Total atoms total_atoms22695
Residues n_residues1575
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax39.0 Å
Rg (real space) rg_real12.81 Å
Rg uncertainty (real space) rg_real_error0.31 Å
I(0) (real space) i0_real4.6480e+08
I(0) uncertainty (real space) i0_real_error5.1720e+06
Rg (reciprocal space) rg_reciprocal12.82 Å
I(0) (reciprocal space) i0_reciprocal464800000.0000
Solution quality estimate total_estimate0.8204
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.3 Å
Skewness Skewness skewness0.025
Kurtosis Kurtosis kurtosis-0.368
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha157800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1b9ra_
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.15.4.1 — 2Fe-2S ferredoxin-related

CATH v4.4 (1 domains)

Domain ID domain_id1b9rA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily30 — Beta-grasp domain
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8. Citations (2)

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9. Files and Curves (10)