1mdu

Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)

Method: X-RAY DIFFRACTION Dmax: 129.7 Å Quality: GOOD

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

gelsolin precursor

Homo sapiens

UniProt P06396

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 52–176 Fragment:actin-severing a-actin × 3 (P68139) CA CALCIUM ION × 12 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;PEG 3350, tris, calcium chloride, magnesium chloride, ADP, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.20 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 52–176 Fragment:actin-severing a-actin × 3 (P68139) CA CALCIUM ION × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;PEG 3350, tris, calcium chloride, magnesium chloride, ADP, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.20 Å R-free 0.233

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.

60 other PDB entries and 93 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GELS_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–125; UniProt 52–176 Author chain D; PDBConstruct 1–125; UniProt 52–176

a-actin

OrganismNot specified

UniProt P68139

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) gelsolin precursor × 3 (P06396) CA CALCIUM ION × 12 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;PEG 3350, tris, calcium chloride, magnesium chloride, ADP, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.20 Å R-free 0.233
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) gelsolin precursor × 3 (P06396) CA CALCIUM ION × 9 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;PEG 3350, tris, calcium chloride, magnesium chloride, ADP, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.20 Å R-free 0.233

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.

57 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_CHICK
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–377; UniProt 1–377 Author chain E; PDBConstruct 1–377; UniProt 1–377

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 1mdu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mdu
Deposition date deposition_date2002-08-07
Structure title titleCrystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)
Keywords keywords;gelsolin precursor, a-actin, ADENOSINE-5'-TRIPHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1, 3-DIOL, 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_guinier38.26
Radius of gyration Rg (electron density) rg_electron38.12
Forward intensity I(0) i0182586000.00
Molecular weight molecular_weight109460.0 kDa
Excluded volume excluded_volume136830 ų
Envelope volume envelope_volume176780 ų
Hydration-shell volume shell_volume40285 ų
Envelope diameter envelope_diameter137.9
Shell Rg shell_rg41.96
Envelope Rg envelope_rg37.73
Shape Rg shape_rg38.12
Total Rg total_rg38.33
Total atoms total_atoms7688
Residues n_residues968
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 dmax129.7
Rg (real space) rg_real38.57
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real1.8260e+08
I(0) uncertainty (real space) i0_real_error3.2110e+06
Rg (reciprocal space) rg_reciprocal38.39
I(0) (reciprocal space) i0_reciprocal182600000.0000
Solution quality estimate total_estimate0.8406
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.8
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21650000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.817; Smooth: 0.656

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1mdua_
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.109.1.1 — Gelsolin-like
Domain ID domain_idd1mdub1
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_idd1mdub2
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_idd1mdud_
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.109.1.1 — Gelsolin-like
Domain ID domain_idd1mdue1
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_idd1mdue2
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

CATH v4.4 (10 domains)

Domain ID domain_id1mduA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id1mduB01
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_id1mduB02
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_id1mduB03
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_id1mduB04
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_id1mduD00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id1mduE01
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_id1mduE02
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_id1mduE03
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_id1mduE04
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

8. Citations (1)

9. Files and Curves (10)