4iq4

Structure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, P21212 form

Method: X-RAY DIFFRACTION Dmax: 153.1 Å Quality: GOOD

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

Non-haem bromoperoxidase BPO-A2, Matrix protein 1

Influenza A virus

UniProt P03485

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 3–165 Chain B; UniProt 3–165 Chain C; UniProt 3–165 Chain D; UniProt 3–165 Chain E; UniProt 3–165 Chain F; UniProt 3–165 Mutation:K118A, L279Q, Q24T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.4;298 K;0.1M Na Citrate pH 4.4, 10% PEG 3,000, vapor diffusion, hanging drop, temperature 298K Resolution 3.50 Å R-free 0.231

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.

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

View Construct and Data Evidence
UniProt name M1_I34A1
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 287–449; UniProt 3–165 Author chain B; PDBConstruct 287–449; UniProt 3–165 Author chain C; PDBConstruct 287–449; UniProt 3–165 Author chain D; PDBConstruct 287–449; UniProt 3–165 Author chain E; PDBConstruct 287–449; UniProt 3–165 Author chain F; PDBConstruct 287–449; UniProt 3–165

Non-haem bromoperoxidase BPO-A2, Matrix protein 1

Influenza A virus

UniProt P29715

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–278 Chain B; UniProt 1–278 Chain C; UniProt 1–278 Chain D; UniProt 1–278 Chain E; UniProt 1–278 Chain F; UniProt 1–278 Mutation:K118A, L279Q, Q24T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.4;298 K;0.1M Na Citrate pH 4.4, 10% PEG 3,000, vapor diffusion, hanging drop, temperature 298K Resolution 3.50 Å R-free 0.231

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.

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BPOA2_STRAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–278; UniProt 1–278 Author chain B; PDBConstruct 1–278; UniProt 1–278 Author chain C; PDBConstruct 1–278; UniProt 1–278 Author chain D; PDBConstruct 1–278; UniProt 1–278 Author chain E; PDBConstruct 1–278; UniProt 1–278 Author chain F; PDBConstruct 1–278; UniProt 1–278

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 4iq4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4iq4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4iq4
Deposition date deposition_date2013-01-10
Structure title titleStructure of a 16 nm protein cage designed by fusing symmetric oligomeric domains, triple mutant, P21212 form
Keywords keywordsprotein design, bionanotechnology, protein assembly, symmetric oligomeric domains, biomaterials, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier50.14
Radius of gyration Rg (electron density) rg_electron49.69
Forward intensity I(0) i01162570000.00
Molecular weight molecular_weight288400.0 kDa
Excluded volume excluded_volume362010 ų
Envelope volume envelope_volume519950 ų
Hydration-shell volume shell_volume84734 ų
Envelope diameter envelope_diameter147.2
Shell Rg shell_rg57.54
Envelope Rg envelope_rg47.16
Shape Rg shape_rg49.71
Total Rg total_rg49.88
Total atoms total_atoms20388
Residues n_residues2640
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 dmax153.1
Rg (real space) rg_real49.95
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real1.1630e+09
I(0) uncertainty (real space) i0_real_error1.9850e+07
Rg (reciprocal space) rg_reciprocal50.28
I(0) (reciprocal space) i0_reciprocal1163000000.0000
Solution quality estimate total_estimate0.8944
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.3
Skewness Skewness skewness0.026
Kurtosis Kurtosis kurtosis-0.751
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha58280000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.968; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.728

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 18 domains

CATH v4.4 (18 domains)

Domain ID domain_id4iq4A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id4iq4A02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Influenza matrix M1, N-terminal subdomain 1
Domain ID domain_id4iq4A03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily180 — Influenza matrix protein M1, N-terminal subdomain 2
Domain ID domain_id4iq4B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id4iq4B02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Influenza matrix M1, N-terminal subdomain 1
Domain ID domain_id4iq4B03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily180 — Influenza matrix protein M1, N-terminal subdomain 2
Domain ID domain_id4iq4C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id4iq4C02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Influenza matrix M1, N-terminal subdomain 1
Domain ID domain_id4iq4C03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily180 — Influenza matrix protein M1, N-terminal subdomain 2
Domain ID domain_id4iq4D01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id4iq4D02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Influenza matrix M1, N-terminal subdomain 1
Domain ID domain_id4iq4D03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily180 — Influenza matrix protein M1, N-terminal subdomain 2
Domain ID domain_id4iq4E01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id4iq4E02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Influenza matrix M1, N-terminal subdomain 1
Domain ID domain_id4iq4E03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily180 — Influenza matrix protein M1, N-terminal subdomain 2
Domain ID domain_id4iq4F01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id4iq4F02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Influenza matrix M1, N-terminal subdomain 1
Domain ID domain_id4iq4F03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily180 — Influenza matrix protein M1, N-terminal subdomain 2

8. Citations (1)

9. Files and Curves (10)