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1r21

Solution Structure of human Ki67 FHA Domain

Method: SOLUTION NMR Dmax: 44.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Antigen Ki-67

Homo sapiens

UniProt P46013

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 1–120 Fragment：FHA domain Mutation：none No other associated polymer SOLUTION NMR NMR measurement conditions：pH 8.4；290 K；Ionic strength (raw mmCIF value) 0；Pressure ambient NMR measurement conditions：pH 7.5；290 K；Ionic strength (raw mmCIF value) 150 mM NaCl；Pressure ambient NMR sample composition：0.5 mM U-13C,15N-protein; 10 mM TrisHCl buffer (pH 8.4); 2mM DTT; 1 mM EDTA | 95% H2O, 10% D2O NMR sample composition：0.5 mM U-13C,15N-protein; 5 mM HEPES buffer (pH 7.5); 2mM DTT; 1 mM EDTA; 150 mM NaCl | 95% H2O, 10% D2O NMR sample composition：0.5 mM unlabeled-protein; 10 mM TrisHCl buffer (pH 8.4); 2mM DTT; 1 mM EDTA | 95% H2O, 10% D2O NMR sample composition：0.5 mM unlabeled-protein; 10 mM TrisHCl buffer (pH 8.4); 2mM DTT; 1 mM EDTA | 100% 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.

Other PDB Difference from Current Entry 1R21 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
2AFF The solution structure of the Ki67FHA/hNIFK(226-269)3P complex Deposited 2005-07-25 Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–120（120 aa） Fragment：FHA domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；293 K；Ionic strength (raw mmCIF value) 150 mM NaCl；Pressure ambient
NMR sample composition 0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 93% H2O/7% D2O
NMR sample composition 0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 100% D2O
NMR sample composition 1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 93% H2O/7% D2O
NMR sample composition 1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 100% D2O
Resolution not provided
5J28 Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex Deposited 2016-03-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 496–536（41 aa） Fragment：UNP residues 496-536
Mutation：T525M MLI MALONATE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；1.9 M Sodium Malonate pH 4.0
Resolution 2.00 Å R-free 0.197
5J28 Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex Deposited 2016-03-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 496–536（41 aa） Fragment：UNP residues 496-536
Mutation：T525M MLI MALONATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；277 K；1.9 M Sodium Malonate pH 4.0
Resolution 2.00 Å R-free 0.197

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KI67_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 9–128； UniProt 1–120

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 1r21

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1r21
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1r21
Deposition date deposition_date2003-09-25
Structure title titleSolution Structure of human Ki67 FHA Domain
Keywords keywordsbeta sandwich, CELL CYCLE; CELL CYCLE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier13.24 Å
Radius of gyration Rg (electron density) rg_electron13.01 Å
Forward intensity I(0) i0979416000.00
Molecular weight molecular_weight262320.0 kDa
Excluded volume excluded_volume327350 ų
Envelope volume envelope_volume25684 ų
Hydration-shell volume shell_volume14145 ų
Envelope diameter envelope_diameter51.4 Å
Shell Rg shell_rg21.37 Å
Envelope Rg envelope_rg15.92 Å
Shape Rg shape_rg12.98 Å
Total Rg total_rg13.26 Å
Total atoms total_atoms37076
Residues n_residues2300
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 dmax44.4 Å
Rg (real space) rg_real13.14 Å
Rg uncertainty (real space) rg_real_error0.29 Å
I(0) (real space) i0_real9.7940e+08
I(0) uncertainty (real space) i0_real_error9.0070e+06
Rg (reciprocal space) rg_reciprocal13.15 Å
I(0) (reciprocal space) i0_reciprocal979400000.0000
Solution quality estimate total_estimate0.7842
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.3 Å
Skewness Skewness skewness0.112
Kurtosis Kurtosis kurtosis-0.240
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha244300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.731; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; 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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1r21a_
Class classb — All beta proteins
Fold Fold foldb.26 — SMAD/FHA domain
Superfamily Superfamily superfamilyb.26.1 — SMAD/FHA domain
Family Family familyb.26.1.2 — FHA domain

CATH v4.4 (1 domains)

Domain ID domain_id1r21A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology200 — Tumour Suppressor Smad4
Homologous superfamily homologous superfamily20 —
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8. Citations (1)

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9. Files and Curves (10)