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1cnu

PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA

Method: X-RAY DIFFRACTION Dmax: 54.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ACTOPHORIN

Acanthamoeba polyphaga

UniProt P37167

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 2–137 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 8；pH 8.0 Resolution 2.25 Å R-free 0.304

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 1CNU Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AHQ RECOMBINANT ACTOPHORIN Deposited 1997-04-10 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–137（137 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；20-25% PEG 8000, 100MM HEPES (PH7.5), 10% ISOPROPANOL, 1MM DTT
Resolution 2.30 Å R-free 0.320
7RTX Actophorin grown in microgravity Deposited 2021-08-16 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–138（137 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；298 K；10 mg/mL protein, 0.1 M MOPS, 16% Polyethylene glycol (8,000)
Resolution 1.65 Å R-free 0.223
7SOG Thermostable actophorin Deposited 2021-10-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–135（134 aa）
Mutation：S2P, H21K, Q22K, T27I, M30L, A32D, S33D, H41K, K53L, S54A, R59N, Q71E, T81V, T99A, T101S, S104A, V110D, A122D, S130K NI NICKEL (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；PEG 8000, NISO4, MES pH6.5
Resolution 1.74 Å R-free 0.225
7SOG Thermostable actophorin Deposited 2021-10-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 2–135（134 aa）
Mutation：S2P, H21K, Q22K, T27I, M30L, A32D, S33D, H41K, K53L, S54A, R59N, Q71E, T81V, T99A, T101S, S104A, V110D, A122D, S130K NI NICKEL (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；PEG 8000, NISO4, MES pH6.5
Resolution 1.74 Å R-free 0.225

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTP_ACACA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–137； UniProt 2–137

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 1cnu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cnu
Deposition date deposition_date1999-05-24
Structure title titlePHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA
Keywords keywordsACTIN-BINDING PROTEIN, ADF, COFILIN, CONTRACTILE; CONTRACTILE
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_guinier15.75 Å
Radius of gyration Rg (electron density) rg_electron14.30 Å
Forward intensity I(0) i04569290.00
Molecular weight molecular_weight14989.0 kDa
Excluded volume excluded_volume18671 ų
Envelope volume envelope_volume20907 ų
Hydration-shell volume shell_volume12532 ų
Envelope diameter envelope_diameter52.5 Å
Shell Rg shell_rg20.01 Å
Envelope Rg envelope_rg14.68 Å
Shape Rg shape_rg14.24 Å
Total Rg total_rg15.60 Å
Total atoms total_atoms1054
Residues n_residues134
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 dmax54.8 Å
Rg (real space) rg_real15.68 Å
Rg uncertainty (real space) rg_real_error0.40 Å
I(0) (real space) i0_real4.5690e+06
I(0) uncertainty (real space) i0_real_error5.6630e+04
Rg (reciprocal space) rg_reciprocal15.69 Å
I(0) (reciprocal space) i0_reciprocal4569000.0000
Solution quality estimate total_estimate0.7747
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8 Å
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.164
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1031000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.694; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; 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) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1cnua_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.109 — Gelsolin-like
Superfamily Superfamily superfamilyd.109.1 — Actin depolymerizing proteins
Family Family familyd.109.1.2 — Cofilin-like

CATH v4.4 (1 domains)

Domain ID domain_id1cnuA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
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8. Citations (1)

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9. Files and Curves (10)