1gpx

C85S GAPDX, NMR, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 39.4 Å Quality: GOOD

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

PUTIDAREDOXIN

Pseudomonas putida

UniProt P00259

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 1–106 Mutation:C85S GA GALLIUM (III) ION × 1 SOLUTION NMR NMR measurement conditions:pH 7.4;298 K;Ionic strength (raw mmCIF value) 0.01M;Pressure 1 NMR sample composition:90/10 H2O/D2O 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.

19 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PUTX_PSEPU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–106; UniProt 1–106

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 1gpx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1gpx
Deposition date deposition_date1998-06-10
Structure title titleC85S GAPDX, NMR, 20 STRUCTURES
Keywords keywordsELECTRON TRANSPORT, GAPDX C85S, 20 STRUCTURES ALIGNED AND SA; ELECTRON TRANSPORT
Experimental Method methodSOLUTION NMR

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.50
Radius of gyration Rg (electron density) rg_electron12.29
Forward intensity I(0) i0830556000.00
Molecular weight molecular_weight229290.0 kDa
Excluded volume excluded_volume280530 ų
Envelope volume envelope_volume21155 ų
Hydration-shell volume shell_volume12786 ų
Envelope diameter envelope_diameter47.2
Shell Rg shell_rg19.82
Envelope Rg envelope_rg14.26
Shape Rg shape_rg12.33
Total Rg total_rg12.29
Total atoms total_atoms31300
Residues n_residues2120
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax39.4
Rg (real space) rg_real12.40
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real8.3060e+08
I(0) uncertainty (real space) i0_real_error8.4710e+06
Rg (reciprocal space) rg_reciprocal12.40
I(0) (reciprocal space) i0_reciprocal830600000.0000
Solution quality estimate total_estimate0.8818
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.0
Skewness Skewness skewness-0.003
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha203200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1gpxa_
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_id1gpxA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily30 — Beta-grasp domain

8. Citations (3)

9. Files and Curves (10)