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1aoa

N-TERMINAL ACTIN-CROSSLINKING DOMAIN FROM HUMAN FIMBRIN

Method: X-RAY DIFFRACTION Dmax: 65.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

T-FIMBRIN

OrganismNot specified

UniProt P13797

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 98–372 Fragment：ABD1 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；PROTEIN WAS CRYSTALLIZED FROM 8-20: PEG 8000, 20 MM CALCIUM ACETATE, 100MM SODIUM CACODYLATE, PH 6.5 Resolution 2.40 Å R-free 0.285

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 1AOA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1WJO Solution structure of the forth CH domain from human plastin 3 T-isoform Deposited 2004-05-29 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 517–627（111 aa） Fragment：CH domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient
NMR sample composition 1.16mM CH domain U-15N,13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O | 90% H2O/10% D2O
Resolution not provided
7R94 T-Plastin-F-actin complex Deposited 2021-06-28 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 × 8 PDB declaration: octameric
Chain F 1–630（630 aa）
Chain G 1–630（630 aa）
Chain H 1–630（630 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
7SX8 T-Plastin-F-actin complex, parallel bundled state Deposited 2021-11-22 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain D 1–630（630 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.00 Å
7SX9 T-Plastin-F-actin complex, anti-parallel bundled state Deposited 2021-11-22 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain D 1–630（630 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 10.00 Å
7SXA T-Plastin-F-actin complex, pre-bundling intermediate state Deposited 2021-11-22 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–630（630 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.87 Å

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

View Construct and Data Evidence
UniProt name PLST_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–275； UniProt 98–372

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 1aoa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1aoa
Deposition date deposition_date1997-06-30
Structure title titleN-TERMINAL ACTIN-CROSSLINKING DOMAIN FROM HUMAN FIMBRIN
Keywords keywordsACTIN-BINDING PROTEIN, CALCIUM-BINDING, PHOSPHORYLATION; ACTIN-BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.56 Å
Radius of gyration Rg (electron density) rg_electron19.50 Å
Forward intensity I(0) i012935900.00
Molecular weight molecular_weight27073.0 kDa
Excluded volume excluded_volume33951 ų
Envelope volume envelope_volume40947 ų
Hydration-shell volume shell_volume18010 ų
Envelope diameter envelope_diameter64.5 Å
Shell Rg shell_rg25.01 Å
Envelope Rg envelope_rg19.63 Å
Shape Rg shape_rg19.49 Å
Total Rg total_rg20.33 Å
Total atoms total_atoms1908
Residues n_residues247
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 dmax65.0 Å
Rg (real space) rg_real20.52 Å
Rg uncertainty (real space) rg_real_error0.50 Å
I(0) (real space) i0_real1.2940e+07
I(0) uncertainty (real space) i0_real_error1.6900e+05
Rg (reciprocal space) rg_reciprocal20.53 Å
I(0) (reciprocal space) i0_reciprocal12940000.0000
Solution quality estimate total_estimate0.8250
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6 Å
Skewness Skewness skewness0.254
Kurtosis Kurtosis kurtosis-0.484
Angular range angular_range— – 0.3850 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2106000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; 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) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1aoaa1
Class classa — All alpha proteins
Fold Fold folda.40 — CH domain-like
Superfamily Superfamily superfamilya.40.1 — Calponin-homology domain, CH-domain
Family Family familya.40.1.1 — Calponin-homology domain, CH-domain
Domain ID domain_idd1aoaa2
Class classa — All alpha proteins
Fold Fold folda.40 — CH domain-like
Superfamily Superfamily superfamilya.40.1 — Calponin-homology domain, CH-domain
Family Family familya.40.1.1 — Calponin-homology domain, CH-domain

CATH v4.4 (2 domains)

Domain ID domain_id1aoaA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily10 — Calponin-like domain
Domain ID domain_id1aoaA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology418 — Actin-binding Protein, T-fimbrin; domain 1
Homologous superfamily homologous superfamily10 — Calponin-like domain
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8. Citations (1)

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9. Files and Curves (10)