5adx

CryoEM structure of dynactin complex at 4.0 angstrom resolution

Method: ELECTRON MICROSCOPY Dmax: 273.0 Å Quality: EXCELLENT

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

ACTIN RELATED PROTEIN 1

OrganismNot specified

UniProt F2Z5G5

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain A; UniProt 7–376 Chain B; UniProt 7–376 Chain C; UniProt 7–376 Chain D; UniProt 7–376 Chain E; UniProt 7–376 Chain F; UniProt 7–376 Chain G; UniProt 7–376 Chain I; UniProt 7–376 Not recorded ACTIN, CYTOPLASMIC 1 × 1 (Q6QAQ1) ACTIN RELATED PROTEIN 11 × 1 (I3LHK5) CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 (A0PFK5) F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 (D2JYW4) DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN 5 × 1 (D0G6S1) DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT;pH 6.5;50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ENTHANE Resolution 4.00 Å

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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name F2Z5G5_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–370; UniProt 7–376 Author chain B; PDBConstruct 1–370; UniProt 7–376 Author chain C; PDBConstruct 1–370; UniProt 7–376 Author chain D; PDBConstruct 1–370; UniProt 7–376 Author chain E; PDBConstruct 1–370; UniProt 7–376 Author chain F; PDBConstruct 1–370; UniProt 7–376 Author chain G; PDBConstruct 1–370; UniProt 7–376 Author chain I; PDBConstruct 1–370; UniProt 7–376

ACTIN, CYTOPLASMIC 1

OrganismNot specified

UniProt Q6QAQ1

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain H; UniProt 6–375 Not recorded ACTIN RELATED PROTEIN 1 × 8 (F2Z5G5) ACTIN RELATED PROTEIN 11 × 1 (I3LHK5) CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 (A0PFK5) F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 (D2JYW4) DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN 5 × 1 (D0G6S1) DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT;pH 6.5;50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ENTHANE Resolution 4.00 Å

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–370; UniProt 6–375

ACTIN RELATED PROTEIN 11

OrganismNot specified

UniProt I3LHK5

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain J; UniProt 1–417 Not recorded ACTIN RELATED PROTEIN 1 × 8 (F2Z5G5) ACTIN, CYTOPLASMIC 1 × 1 (Q6QAQ1) CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 (A0PFK5) F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 (D2JYW4) DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN 5 × 1 (D0G6S1) DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT;pH 6.5;50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ENTHANE Resolution 4.00 Å

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 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name I3LHK5_PIG
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–417; UniProt 1–417

CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1

OrganismNot specified

UniProt A0PFK5

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain K; UniProt 7–281 Not recorded ACTIN RELATED PROTEIN 1 × 8 (F2Z5G5) ACTIN, CYTOPLASMIC 1 × 1 (Q6QAQ1) ACTIN RELATED PROTEIN 11 × 1 (I3LHK5) F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 (D2JYW4) DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN 5 × 1 (D0G6S1) DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT;pH 6.5;50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ENTHANE Resolution 4.00 Å

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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0PFK5_PIG
Isoform
PDB entities 4
Chains and sequence ranges Author chain K; PDBConstruct 1–275; UniProt 7–281

F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II

OrganismNot specified

UniProt D2JYW4

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain L; UniProt 2–271 Not recorded ACTIN RELATED PROTEIN 1 × 8 (F2Z5G5) ACTIN, CYTOPLASMIC 1 × 1 (Q6QAQ1) ACTIN RELATED PROTEIN 11 × 1 (I3LHK5) CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 (A0PFK5) DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN 5 × 1 (D0G6S1) DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT;pH 6.5;50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ENTHANE Resolution 4.00 Å

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.

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

View Construct and Data Evidence
UniProt name D2JYW4_PIG
Isoform
PDB entities 5
Chains and sequence ranges Author chain L; PDBConstruct 1–270; UniProt 2–271

DYNACTIN 5

OrganismNot specified

UniProt D0G6S1

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 × 27 PDB declaration: 27-meric(27) Consistent with protein copy count Chain U; UniProt 1–190 Not recorded ACTIN RELATED PROTEIN 1 × 8 (F2Z5G5) ACTIN, CYTOPLASMIC 1 × 1 (Q6QAQ1) ACTIN RELATED PROTEIN 11 × 1 (I3LHK5) CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 (A0PFK5) F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 (D2JYW4) DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 3 × 2 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 6 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 2 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 DYNACTIN SUBUNIT 2 × 1 ELECTRON MICROSCOPY cryo-EM buffer:50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT;pH 6.5;50MM KCL, 25MM K2HPO4- KH2PO4, 1MM MGCL2,5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ENTHANE Resolution 4.00 Å

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.

20 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0G6S1_PIG
Isoform
PDB entities 10
Chains and sequence ranges Author chain U; PDBConstruct 1–189; UniProt 1–190

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 5adx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5adx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5adx
Deposition date deposition_date2015-08-24
Structure title titleCryoEM structure of dynactin complex at 4.0 angstrom resolution
Keywords keywordsSTRUCTURAL PROTEIN, DYNEIN CO-FACTOR, ACTIN-LIKE FILAMENT, CELLULAR CARGO TRANSPORT; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier98.41
Radius of gyration Rg (electron density) rg_electron99.99
Forward intensity I(0) i07419020000.00
Molecular weight molecular_weight697960.0 kDa
Excluded volume excluded_volume858580 ų
Envelope volume envelope_volume1715300 ų
Hydration-shell volume shell_volume161130 ų
Envelope diameter envelope_diameter381.8
Shell Rg shell_rg72.05
Envelope Rg envelope_rg100.20
Shape Rg shape_rg100.10
Total Rg total_rg99.28
Total atoms total_atoms49392
Residues n_residues7306
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 dmax273.0
Rg (real space) rg_real91.84
Rg uncertainty (real space) rg_real_error1.43
I(0) (real space) i0_real7.0830e+09
I(0) uncertainty (real space) i0_real_error1.5290e+08
Rg (reciprocal space) rg_reciprocal89.69
I(0) (reciprocal space) i0_reciprocal7213000000.0000
Solution quality estimate total_estimate0.9097
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.2
Skewness Skewness skewness0.411
Kurtosis Kurtosis kurtosis-0.678
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.7685
Highest regularization parameter α highest_alpha241500000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.014; Oscil: 0.966; Stabil: 0.978; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (17)

7. Fold Classification (SCOP + CATH) 34 domains

CATH v4.4 (34 domains)

Domain ID domain_id5adxA01
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_id5adxA02
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_id5adxA03
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_id5adxB01
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_id5adxB02
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_id5adxB03
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_id5adxC01
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_id5adxC02
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_id5adxC03
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_id5adxD01
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_id5adxD02
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_id5adxD03
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_id5adxE01
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_id5adxE02
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_id5adxE03
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_id5adxF01
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_id5adxF02
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_id5adxF03
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_id5adxG01
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_id5adxG02
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_id5adxG03
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_id5adxH01
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_id5adxH02
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_id5adxH03
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_id5adxI01
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_id5adxI02
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_id5adxI03
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_id5adxJ01
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_id5adxK01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1140 — Ribosomal protein S3 C-terminal domain
Homologous superfamily homologous superfamily60 — F-actin capping protein, alpha subunit
Domain ID domain_id5adxK02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily210 — F-actin capping protein, beta subunit
Domain ID domain_id5adxL01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily570 — F-actin capping protein, alpha/beta subunit, N-terminal domain
Domain ID domain_id5adxL02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily210 — F-actin capping protein, beta subunit
Domain ID domain_id5adxU00
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology10 — UDP N-Acetylglucosamine Acyltransferase; domain 1
Homologous superfamily homologous superfamily10 — Hexapeptide repeat proteins
Domain ID domain_id5adxV00
Class class2 — Mainly Beta
Architecture architecture160 — 3 Solenoid
Topology topology10 — UDP N-Acetylglucosamine Acyltransferase; domain 1
Homologous superfamily homologous superfamily10 — Hexapeptide repeat proteins

8. Citations (1)

9. Files and Curves (10)