2p9s

Structure of bovine Arp2/3 complex co-crystallized with ATP/Mg2+

Method: X-RAY DIFFRACTION Dmax: 141.3 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Actin-like protein 3

Bos taurus

UniProt P61157

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–418 Not recorded Actin-like protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (Q3SYX9) MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;7.5% PEG3350 50mM HEPES 100mM KSCN 10% Sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.68 Å R-free 0.261

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.

28 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP3_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–418; UniProt 1–418

Actin-like protein 2

Bos taurus

UniProt A7MB62

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 1–394 Not recorded Actin-like protein 3 × 1 (P61157) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (Q3SYX9) MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;7.5% PEG3350 50mM HEPES 100mM KSCN 10% Sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.68 Å R-free 0.261

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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARP2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–394; UniProt 1–394

Actin-related protein 2/3 complex subunit 1B

Bos taurus

UniProt Q58CQ2

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 1–372 Not recorded Actin-like protein 3 × 1 (P61157) Actin-like protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (Q3SYX9) MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;7.5% PEG3350 50mM HEPES 100mM KSCN 10% Sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.68 Å R-free 0.261

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.

21 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARC1B_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–372; UniProt 1–372

Actin-related protein 2/3 complex subunit 2

Bos taurus

UniProt Q3MHR7

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain D; UniProt 1–300 Not recorded Actin-like protein 3 × 1 (P61157) Actin-like protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (Q3SYX9) MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;7.5% PEG3350 50mM HEPES 100mM KSCN 10% Sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.68 Å R-free 0.261

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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC2_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–300; UniProt 1–300

Actin-related protein 2/3 complex subunit 3

Bos taurus

UniProt Q3T035

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 1–178 Not recorded Actin-like protein 3 × 1 (P61157) Actin-like protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) Actin-related protein 2/3 complex subunit 5 × 1 (Q3SYX9) MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;7.5% PEG3350 50mM HEPES 100mM KSCN 10% Sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.68 Å R-free 0.261

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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC3_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–178; UniProt 1–178

Actin-related protein 2/3 complex subunit 4

Bos taurus

UniProt Q148J6

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain F; UniProt 1–168 Not recorded Actin-like protein 3 × 1 (P61157) Actin-like protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 5 × 1 (Q3SYX9) MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;7.5% PEG3350 50mM HEPES 100mM KSCN 10% Sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.68 Å R-free 0.261

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.

26 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC4_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–168; UniProt 1–168

Actin-related protein 2/3 complex subunit 5

Bos taurus

UniProt Q3SYX9

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain G; UniProt 1–151 Not recorded Actin-like protein 3 × 1 (P61157) Actin-like protein 2 × 1 (A7MB62) Actin-related protein 2/3 complex subunit 1B × 1 (Q58CQ2) Actin-related protein 2/3 complex subunit 2 × 1 (Q3MHR7) Actin-related protein 2/3 complex subunit 3 × 1 (Q3T035) Actin-related protein 2/3 complex subunit 4 × 1 (Q148J6) MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;7.5% PEG3350 50mM HEPES 100mM KSCN 10% Sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.68 Å R-free 0.261

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.

24 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARPC5_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–151; UniProt 1–151

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 2p9s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2p9s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2p9s
Deposition date deposition_date2007-03-26
Structure title titleStructure of bovine Arp2/3 complex co-crystallized with ATP/Mg2+
Keywords keywordsactin, WD repeat, complex, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier43.47
Radius of gyration Rg (electron density) rg_electron43.11
Forward intensity I(0) i0526633000.00
Molecular weight molecular_weight190010.0 kDa
Excluded volume excluded_volume238100 ų
Envelope volume envelope_volume316870 ų
Hydration-shell volume shell_volume61042 ų
Envelope diameter envelope_diameter145.8
Shell Rg shell_rg48.17
Envelope Rg envelope_rg42.69
Shape Rg shape_rg43.11
Total Rg total_rg43.34
Total atoms total_atoms13375
Residues n_residues1690
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax141.3
Rg (real space) rg_real44.79
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real5.2350e+08
I(0) uncertainty (real space) i0_real_error7.7060e+06
Rg (reciprocal space) rg_reciprocal43.47
I(0) (reciprocal space) i0_reciprocal526700000.0000
Solution quality estimate total_estimate0.6962
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.2
Skewness Skewness skewness0.308
Kurtosis Kurtosis kurtosis-0.514
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha1.8750
Highest regularization parameter α highest_alpha71220000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 0.899; Sysdev: 0.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.577

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

7. Fold Classification (SCOP + CATH) 21 domains

SCOP 2.08 (9 domains)

Domain ID domain_idd2p9sa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd2p9sa2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd2p9sb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd2p9sc_
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.4 — WD40 repeat-like
Family Family familyb.69.4.1 — WD40-repeat
Domain ID domain_idd2p9sd1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.198 — Secretion chaperone-like
Superfamily Superfamily superfamilyd.198.2 — Arp2/3 complex subunits
Family Family familyd.198.2.1 — Arp2/3 complex subunits
Domain ID domain_idd2p9sd2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.198 — Secretion chaperone-like
Superfamily Superfamily superfamilyd.198.2 — Arp2/3 complex subunits
Family Family familyd.198.2.1 — Arp2/3 complex subunits
Domain ID domain_idd2p9se_
Class classa — All alpha proteins
Fold Fold folda.148 — Arp2/3 complex 21 kDa subunit ARPC3
Superfamily Superfamily superfamilya.148.1 — Arp2/3 complex 21 kDa subunit ARPC3
Family Family familya.148.1.1 — Arp2/3 complex 21 kDa subunit ARPC3
Domain ID domain_idd2p9sf_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.198 — Secretion chaperone-like
Superfamily Superfamily superfamilyd.198.2 — Arp2/3 complex subunits
Family Family familyd.198.2.1 — Arp2/3 complex subunits
Domain ID domain_idd2p9sg_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.13 — Arp2/3 complex 16 kDa subunit ARPC5
Family Family familya.118.13.1 — Arp2/3 complex 16 kDa subunit ARPC5

CATH v4.4 (12 domains)

Domain ID domain_id2p9sA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id2p9sA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology36 — Actin; Chain A, domain 2
Homologous superfamily homologous superfamily70 — Actin; Chain A, domain 2
Domain ID domain_id2p9sA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id2p9sA04
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id2p9sB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id2p9sB02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id2p9sC00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id2p9sD01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1460 — Yope Regulator; Chain: A,
Homologous superfamily homologous superfamily20
Domain ID domain_id2p9sD02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1460 — Yope Regulator; Chain: A,
Homologous superfamily homologous superfamily20
Domain ID domain_id2p9sE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1760 — Arp2/3 complex 21 kDa subunit ARPC3
Homologous superfamily homologous superfamily10 — Actin-related protein 2/3 complex subunit 3
Domain ID domain_id2p9sF00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1460 — Yope Regulator; Chain: A,
Homologous superfamily homologous superfamily20
Domain ID domain_id2p9sG00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily190 — Actin-related protein 2/3 complex subunit 5

8. Citations (1)

9. Files and Curves (10)