5afu

Cryo-EM structure of dynein tail-dynactin-BICD2N complex

Method: ELECTRON MICROSCOPY Dmax: 266.9 Å Quality: EXCELLENT

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

DYNACTIN

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 × 33 PDB declaration: 33-meric(33) 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 DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 ACTIN, CYTOPLASMIC 1 × 1 (Q6QAQ1) DYNACTIN × 1 (I3LHK5) CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 (A0PFK5) F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 (D2JYW4) DYNACTIN × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT;pH 7.4;150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 8.20 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 5
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 × 33 PDB declaration: 33-meric(33) Consistent with protein copy count Chain H; UniProt 6–375 Not recorded DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 DYNACTIN × 8 (F2Z5G5) DYNACTIN × 1 (I3LHK5) CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 (A0PFK5) F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 (D2JYW4) DYNACTIN × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT;pH 7.4;150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 8.20 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 6
Chains and sequence ranges Author chain H; PDBConstruct 1–370; UniProt 6–375

DYNACTIN

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 × 33 PDB declaration: 33-meric(33) Consistent with protein copy count Chain J; UniProt 12–390 Not recorded DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 DYNACTIN × 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 × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT;pH 7.4;150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 8.20 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 7
Chains and sequence ranges Author chain J; PDBConstruct 1–379; UniProt 12–390

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 × 33 PDB declaration: 33-meric(33) Consistent with protein copy count Chain K; UniProt 7–281 Not recorded DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 DYNACTIN × 8 (F2Z5G5) ACTIN, CYTOPLASMIC 1 × 1 (Q6QAQ1) DYNACTIN × 1 (I3LHK5) F-ACTIN CAPPING PROTEIN BETA SUBUNIT VARIANT II × 1 (D2JYW4) DYNACTIN × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT;pH 7.4;150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 8.20 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 8
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 × 33 PDB declaration: 33-meric(33) Consistent with protein copy count Chain L; UniProt 2–271 Not recorded DYNEIN TAIL × 1 DYNEIN TAIL × 1 DYNEIN TAIL × 2 DYNEIN TAIL × 2 DYNACTIN × 8 (F2Z5G5) ACTIN, CYTOPLASMIC 1 × 1 (Q6QAQ1) DYNACTIN × 1 (I3LHK5) CAPPING PROTEIN (ACTIN FILAMENT) MUSCLE Z-LINE, ALPHA 1 × 1 (A0PFK5) DYNACTIN × 1 DYNACTIN 6 × 1 DYNACTIN × 2 DYNACTIN × 2 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 DYNACTIN × 1 F-ACTIN-CAPPING PROTEIN SUBUNIT BETA × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT;pH 7.4;150MM KCL, 25MM HEPES-KOH, 1MM MGCL2, 0.1MM MGATP, 5MM DTT cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 8.20 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 9
Chains and sequence ranges Author chain L; PDBConstruct 1–270; UniProt 2–271

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 5afu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5afu
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5afu
Deposition date deposition_date2015-01-26
Structure title titleCryo-EM structure of dynein tail-dynactin-BICD2N complex
Keywords keywordsDYNEIN, DYNACTIN, BICD2, MOTOR, TRANSPORT, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier96.22
Radius of gyration Rg (electron density) rg_electron97.59
Forward intensity I(0) i09926840000.00
Molecular weight molecular_weight790350.0 kDa
Excluded volume excluded_volume964020 ų
Envelope volume envelope_volume1934300 ų
Hydration-shell volume shell_volume184560 ų
Envelope diameter envelope_diameter390.7
Shell Rg shell_rg75.84
Envelope Rg envelope_rg96.02
Shape Rg shape_rg97.66
Total Rg total_rg97.09
Total atoms total_atoms55952
Residues n_residues8572
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 dmax266.9
Rg (real space) rg_real89.99
Rg uncertainty (real space) rg_real_error1.32
I(0) (real space) i0_real9.4870e+09
I(0) uncertainty (real space) i0_real_error2.1760e+08
Rg (reciprocal space) rg_reciprocal89.99
I(0) (reciprocal space) i0_reciprocal9731000000.0000
Solution quality estimate total_estimate0.9159
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary100.1
Skewness Skewness skewness0.385
Kurtosis Kurtosis kurtosis-0.522
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.7057
Highest regularization parameter α highest_alpha352500000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.031; Oscil: 0.993; Stabil: 0.976; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.005

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (24)

7. Fold Classification (SCOP + CATH) 35 domains

CATH v4.4 (35 domains)

Domain ID domain_id5afu300
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_id5afu400
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_id5afuA01
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_id5afuA02
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_id5afuA03
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_id5afuB01
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_id5afuB02
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_id5afuB03
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_id5afuC01
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_id5afuC02
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_id5afuC03
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_id5afuD01
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_id5afuD02
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_id5afuD03
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_id5afuE01
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_id5afuE02
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_id5afuE03
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_id5afuF01
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_id5afuF02
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_id5afuF03
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_id5afuG01
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_id5afuG02
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_id5afuG03
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_id5afuH01
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_id5afuH02
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_id5afuH03
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_id5afuI01
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_id5afuI02
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_id5afuI03
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_id5afuK01
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_id5afuK02
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_id5afuL01
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_id5afuL02
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_id5afuU00
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_id5afuV00
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)