1k8k

Crystal Structure of Arp2/3 Complex

Method: X-RAY DIFFRACTION Dmax: 144.3 Å Quality: GOOD

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

ACTIN-LIKE PROTEIN 3

OrganismNot specified

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) ARP2/3 COMPLEX 41 KDA SUBUNIT × 1 (Q58CQ2) ARP2/3 COMPLEX 34 KDA SUBUNIT × 1 (Q3MHR7) ARP2/3 COMPLEX 21 KDA SUBUNIT × 1 (Q3T035) ARP2/3 COMPLEX 20 KDA SUBUNIT × 1 (Q148J6) ARP2/3 COMPLEX 16 KDA SUBUNIT × 1 (Q3SYX9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;PEG 8000, KSCN, Hepes at pH 7.5, VAPOR DIFFUSION, HANGING DROP at 298K Resolution 2.00 Å R-free 0.251

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

OrganismNot specified

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) ARP2/3 COMPLEX 41 KDA SUBUNIT × 1 (Q58CQ2) ARP2/3 COMPLEX 34 KDA SUBUNIT × 1 (Q3MHR7) ARP2/3 COMPLEX 21 KDA SUBUNIT × 1 (Q3T035) ARP2/3 COMPLEX 20 KDA SUBUNIT × 1 (Q148J6) ARP2/3 COMPLEX 16 KDA SUBUNIT × 1 (Q3SYX9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;PEG 8000, KSCN, Hepes at pH 7.5, VAPOR DIFFUSION, HANGING DROP at 298K Resolution 2.00 Å R-free 0.251

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

ARP2/3 COMPLEX 41 KDA SUBUNIT

OrganismNot specified

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) ARP2/3 COMPLEX 34 KDA SUBUNIT × 1 (Q3MHR7) ARP2/3 COMPLEX 21 KDA SUBUNIT × 1 (Q3T035) ARP2/3 COMPLEX 20 KDA SUBUNIT × 1 (Q148J6) ARP2/3 COMPLEX 16 KDA SUBUNIT × 1 (Q3SYX9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;PEG 8000, KSCN, Hepes at pH 7.5, VAPOR DIFFUSION, HANGING DROP at 298K Resolution 2.00 Å R-free 0.251

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

ARP2/3 COMPLEX 34 KDA SUBUNIT

OrganismNot specified

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) ARP2/3 COMPLEX 41 KDA SUBUNIT × 1 (Q58CQ2) ARP2/3 COMPLEX 21 KDA SUBUNIT × 1 (Q3T035) ARP2/3 COMPLEX 20 KDA SUBUNIT × 1 (Q148J6) ARP2/3 COMPLEX 16 KDA SUBUNIT × 1 (Q3SYX9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;PEG 8000, KSCN, Hepes at pH 7.5, VAPOR DIFFUSION, HANGING DROP at 298K Resolution 2.00 Å R-free 0.251

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

ARP2/3 COMPLEX 21 KDA SUBUNIT

OrganismNot specified

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) ARP2/3 COMPLEX 41 KDA SUBUNIT × 1 (Q58CQ2) ARP2/3 COMPLEX 34 KDA SUBUNIT × 1 (Q3MHR7) ARP2/3 COMPLEX 20 KDA SUBUNIT × 1 (Q148J6) ARP2/3 COMPLEX 16 KDA SUBUNIT × 1 (Q3SYX9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;PEG 8000, KSCN, Hepes at pH 7.5, VAPOR DIFFUSION, HANGING DROP at 298K Resolution 2.00 Å R-free 0.251

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

ARP2/3 COMPLEX 20 KDA SUBUNIT

OrganismNot specified

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) ARP2/3 COMPLEX 41 KDA SUBUNIT × 1 (Q58CQ2) ARP2/3 COMPLEX 34 KDA SUBUNIT × 1 (Q3MHR7) ARP2/3 COMPLEX 21 KDA SUBUNIT × 1 (Q3T035) ARP2/3 COMPLEX 16 KDA SUBUNIT × 1 (Q3SYX9) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;PEG 8000, KSCN, Hepes at pH 7.5, VAPOR DIFFUSION, HANGING DROP at 298K Resolution 2.00 Å R-free 0.251

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

ARP2/3 COMPLEX 16 KDA SUBUNIT

OrganismNot specified

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) ARP2/3 COMPLEX 41 KDA SUBUNIT × 1 (Q58CQ2) ARP2/3 COMPLEX 34 KDA SUBUNIT × 1 (Q3MHR7) ARP2/3 COMPLEX 21 KDA SUBUNIT × 1 (Q3T035) ARP2/3 COMPLEX 20 KDA SUBUNIT × 1 (Q148J6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;PEG 8000, KSCN, Hepes at pH 7.5, VAPOR DIFFUSION, HANGING DROP at 298K Resolution 2.00 Å R-free 0.251

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 1k8k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1k8k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1k8k
Deposition date deposition_date2001-10-24
Structure title titleCrystal Structure of Arp2/3 Complex
Keywords keywordsbeta-propeller, 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_guinier44.27
Radius of gyration Rg (electron density) rg_electron43.85
Forward intensity I(0) i0534833000.00
Molecular weight molecular_weight193340.0 kDa
Excluded volume excluded_volume243140 ų
Envelope volume envelope_volume334380 ų
Hydration-shell volume shell_volume63222 ų
Envelope diameter envelope_diameter149.4
Shell Rg shell_rg48.86
Envelope Rg envelope_rg43.40
Shape Rg shape_rg43.84
Total Rg total_rg44.10
Total atoms total_atoms13616
Residues n_residues1709
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 dmax144.3
Rg (real space) rg_real44.24
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real5.3480e+08
I(0) uncertainty (real space) i0_real_error8.8120e+06
Rg (reciprocal space) rg_reciprocal44.27
I(0) (reciprocal space) i0_reciprocal534900000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.1
Skewness Skewness skewness0.200
Kurtosis Kurtosis kurtosis-0.694
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha79980000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 21 domains

SCOP 2.08 (9 domains)

Domain ID domain_idd1k8ka1
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_idd1k8ka2
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_idd1k8kb1
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_idd1k8kc_
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_idd1k8kd1
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_idd1k8kd2
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_idd1k8ke_
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_idd1k8kf_
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_idd1k8kg_
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_id1k8kA01
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_id1k8kA02
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_id1k8kA03
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_id1k8kA04
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_id1k8kB01
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_id1k8kB02
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_id1k8kC00
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_id1k8kD01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1460 — Yope Regulator; Chain: A,
Homologous superfamily homologous superfamily20
Domain ID domain_id1k8kD02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1460 — Yope Regulator; Chain: A,
Homologous superfamily homologous superfamily20
Domain ID domain_id1k8kE00
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_id1k8kF00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1460 — Yope Regulator; Chain: A,
Homologous superfamily homologous superfamily20
Domain ID domain_id1k8kG00
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 (4)

9. Files and Curves (10)