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1cur

REDUCED RUSTICYANIN, NMR

Method: SOLUTION NMR Dmax: 47.4 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

CU(I) RUSTICYANIN

Acidithiobacillus ferrooxidans

UniProt P24930

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 1–155 Not recorded CU COPPER (II) ION × 1 SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 1CUR Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A3Z REDUCED RUSTICYANIN AT 1.9 ANGSTROMS Deposited 1998-01-27 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–187（155 aa）
Not recorded CU1 COPPER (I) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；VAPOR DIFFUSION IN HANGING DROPS AGAINST 100 MM-SODIUM CITRATE, PH 4.6, 200 MM LITHIUM CHLORIDE AND 25%(W/V) PEG 8000 AT 277K. CRYSTALS SOAKED IN 10MM DITHIONITE FOR 3 DAYS PRIOR TO DATA COLLECTION., vapor diffusion - hanging drop
Resolution 1.90 Å R-free 0.272
1A8Z STRUCTURE DETERMINATION OF A 16.8KDA COPPER PROTEIN RUSTICYANIN AT 2.1A RESOLUTION USING ANOMALOUS SCATTERING DATA WITH DIRECT METHODS Deposited 1998-03-30 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–187（153 aa）
Not recorded CU1 COPPER (I) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 3.8；SIMILAR TO THOSE DESCRIBED IN DJEBLI ET AL., J. MOL. BIOL. 229, 581 (1992)., pH 3.8
Resolution 2.10 Å R-free 0.219
1GY1 Crystal structures of Ser86Asp and Met148Leu Rusticyanin Deposited 2002-04-16 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 33–187（155 aa）
Mutation：YES CU COPPER (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5.00
Resolution 1.65 Å R-free 0.190
1GY1 Crystal structures of Ser86Asp and Met148Leu Rusticyanin Deposited 2002-04-16 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 33–187（155 aa）
Mutation：YES CU COPPER (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5；pH 5.00
Resolution 1.65 Å R-free 0.190
1RCY RUSTICYANIN (RC) FROM THIOBACILLUS FERROOXIDANS Deposited 1996-04-10 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 38–187（150 aa）
Not recorded CU COPPER (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.6；pH 4.6
Resolution 1.90 Å R-free 0.252
2CAK 1.27Angstrom Structure of Rusticyanin from Thiobacillus ferrooxidans Deposited 2005-12-21 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–187（153 aa）
Not recorded CU1 COPPER (I) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 3.8；pH 3.80
Resolution 1.27 Å R-free 0.138
2CAL Crystal structure of His143Met rusticyanin Deposited 2005-12-21 Different construct Different mutation/modification Different ligand/ion Different experimental method Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 35–187（153 aa）
Mutation：YES CU1 COPPER (I) ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.10 Å R-free 0.170

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUS2_THIFE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–155； UniProt 1–155

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 1cur

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cur
Deposition date deposition_date1996-04-19
Structure title titleREDUCED RUSTICYANIN, NMR
Keywords keywordsRUSTICYANIN, TYPE 1 COPPER PROTEIN, SOLUTION STRUCTURE, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier14.06 Å
Radius of gyration Rg (electron density) rg_electron14.20 Å
Forward intensity I(0) i0765866000.00
Molecular weight molecular_weight248980.0 kDa
Excluded volume excluded_volume316480 ų
Envelope volume envelope_volume29641 ų
Hydration-shell volume shell_volume15822 ų
Envelope diameter envelope_diameter49.5 Å
Shell Rg shell_rg21.81 Å
Envelope Rg envelope_rg15.67 Å
Shape Rg shape_rg14.15 Å
Total Rg total_rg14.52 Å
Total atoms total_atoms35175
Residues n_residues2325
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 dmax47.4 Å
Rg (real space) rg_real14.28 Å
Rg uncertainty (real space) rg_real_error0.11 Å
I(0) (real space) i0_real7.5860e+08
I(0) uncertainty (real space) i0_real_error7.7340e+06
Rg (reciprocal space) rg_reciprocal13.94 Å
I(0) (reciprocal space) i0_reciprocal765900000.0000
Solution quality estimate total_estimate0.6636
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.4 Å
Skewness Skewness skewness0.219
Kurtosis Kurtosis kurtosis0.041
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha6.9900
Highest regularization parameter α highest_alpha423800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.777; Stabil: 0.932; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.535
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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_idd1cura_
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.1 — Plastocyanin/azurin-like

CATH v4.4 (1 domains)

Domain ID domain_id1curA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
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8. Citations (4)

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9. Files and Curves (10)