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1aft

SMALL SUBUNIT C-TERMINAL INHIBITORY PEPTIDE OF MOUSE RIBONUCLEOTIDE REDUCTASE AS BOUND TO THE LARGE SUBUNIT, NMR, 26 STRUCTURES

Method: SOLUTION NMR Dmax: 12.2 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE

OrganismNot specified

UniProt P11157

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 384–390 Fragment：C-TERMINAL RESIDUES AC-FTLDADF OF SMALL SUBUNIT Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 7；287 K 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 1AFT Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1H0N Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous state Deposited 2002-06-26 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 1–390（390 aa）
Not recorded CO COBALT (II) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；0.1 M NA-ACETATE BUFFER PH4.7, 1.2 M NACL, 7.5 MG/ML APO-R2 PROTEIN. CRYSTALS WERE SOAKED IN 5 MM CO2+ SOLUTION, PH INCREASED TO 6
Resolution 2.40 Å R-free 0.297
1H0O Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous state Deposited 2002-06-26 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 1–390（390 aa）
Not recorded CO COBALT (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.7；0.1 M NA-ACETATE BUFFER PH4.7, 1.2 M NACL, 7.5 MG/ML APO-R2 PROTEIN. CRYSTALS WERE MADE BY CO-CRYSTALLISATION (3.8 EQV. CO2+)., pH 4.70
Resolution 2.20 Å R-free 0.282
1W68 Crystal Structure of Mouse Ribonucleotide Reductase Subunit R2 under Oxidizing Conditions. A Fully Occupied Dinuclear Iron Cluster. Deposited 2004-08-16 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 1–390（390 aa）
Not recorded FEO MU-OXO-DIIRON × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；0.1 M SODIUM ACETATE PH 4.7, 1.2 M SODIUM CHLORIDE
Resolution 2.20 Å R-free 0.260
1W69 Crystal Structure of Mouse Ribonucleotide Reductase Subunit R2 under Reducing Conditions. A Fully Occupied Dinuclear Iron Cluster and Bound Acetate. Deposited 2004-08-16 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 1–390（390 aa）
Not recorded FE2 FE (II) ION × 4 ACY ACETIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；0.1 M SODIUM ACETATE PH 4.7, 1.2 M SODIUM CHLORIDE
Resolution 2.20 Å R-free 0.272
1XSM PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE FROM MOUSE Deposited 1996-07-03 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 1–390（390 aa）
Not recorded FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.7；1.0-1.2 M NACL, 0.1 M SODIUM ACETATE, PH 4.7, 0-4% PEG4000.
Resolution 2.30 Å R-free 0.250

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RIR2_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–8； UniProt 384–390

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 1aft

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1aft
Deposition date deposition_date1997-03-13
Structure title titleSMALL SUBUNIT C-TERMINAL INHIBITORY PEPTIDE OF MOUSE RIBONUCLEOTIDE REDUCTASE AS BOUND TO THE LARGE SUBUNIT, NMR, 26 STRUCTURES
Keywords keywordsRIBONUCLEOTIDE REDUCTASE, PEPTIDE INHIBITORS, TRANSFERRED NOESY, RESTRAINED MOLECULAR DYNAMICS, NONSTANDARD TYPE I TURN; RIBONUCLEOTIDE REDUCTASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier3.54 Å
Radius of gyration Rg (electron density) rg_electron4.92 Å
Forward intensity I(0) i06363770.00
Molecular weight molecular_weight22592.0 kDa
Excluded volume excluded_volume28605 ų
Envelope volume envelope_volume1475 ų
Hydration-shell volume shell_volume2698 ų
Envelope diameter envelope_diameter19.2 Å
Shell Rg shell_rg9.72 Å
Envelope Rg envelope_rg5.95 Å
Shape Rg shape_rg4.92 Å
Total Rg total_rg5.20 Å
Total atoms total_atoms2964
Residues n_residues182
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 dmax12.2 Å
Rg (real space) rg_real3.85 Å
Rg uncertainty (real space) rg_real_error0.02 Å
I(0) (real space) i0_real6.5180e+06
I(0) uncertainty (real space) i0_real_error3.4020e+04
Rg (reciprocal space) rg_reciprocal3.41 Å
I(0) (reciprocal space) i0_reciprocal6364000.0000
Solution quality estimate total_estimate0.6428
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary4.2 Å
Skewness Skewness skewness0.261
Kurtosis Kurtosis kurtosis-0.647
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha1.8580
Highest regularization parameter α highest_alpha71.5100
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.984; Stabil: 0.885; Sysdev: 0.000; Positv: 1.000; Valcen: 0.779; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1afta_
Class classj — Peptides
Fold Fold foldj.62 — Small subunit C-terminal inhibitory peptide of ribonucleotide reductase
Superfamily Superfamily superfamilyj.62.1 — Small subunit C-terminal inhibitory peptide of ribonucleotide reductase
Family Family familyj.62.1.1 — Small subunit C-terminal inhibitory peptide of ribonucleotide reductase
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8. Citations (1)

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9. Files and Curves (10)