2w88

Plastocyanin variant with N-terminal Methionine - open structure

Method: X-RAY DIFFRACTION Dmax: 62.9 Å Quality: EXCELLENT

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

PLASTOCYANIN

PHORMIDIUM LAMINOSUM

UniProt Q51883

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 35–139 Chain B; UniProt 35–139 Chain C; UniProt 35–139 Not recorded CU COPPER (II) ION × 6 ZN ZINC ION × 14 X-RAY DIFFRACTION X-ray crystallization conditions:0.1 M ZINC ACETATE, 0.4 M SODIUM ACETATE Resolution 2.89 Å R-free 0.223

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.

8 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLAS_PHOLA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–106; UniProt 35–139 Author chain B; PDBConstruct 2–106; UniProt 35–139 Author chain C; PDBConstruct 2–106; UniProt 35–139

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 2w88

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2w88
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2w88
Deposition date deposition_date2009-01-14
Structure title titlePlastocyanin variant with N-terminal Methionine - open structure
Keywords keywordsPROTEIN INTERACTIONS, TRANSPORT, CUPREDOXIN, SELF-ASSEMBLY, METAL-BINDING, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.33
Radius of gyration Rg (electron density) rg_electron20.32
Forward intensity I(0) i022406700.00
Molecular weight molecular_weight35289.0 kDa
Excluded volume excluded_volume43604 ų
Envelope volume envelope_volume51104 ų
Hydration-shell volume shell_volume21034 ų
Envelope diameter envelope_diameter63.0
Shell Rg shell_rg26.49
Envelope Rg envelope_rg20.33
Shape Rg shape_rg20.26
Total Rg total_rg21.28
Total atoms total_atoms2449
Residues n_residues318
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 dmax62.9
Rg (real space) rg_real21.19
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real2.2410e+07
I(0) uncertainty (real space) i0_real_error3.0030e+05
Rg (reciprocal space) rg_reciprocal21.22
I(0) (reciprocal space) i0_reciprocal22410000.0000
Solution quality estimate total_estimate0.9172
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.9
Skewness Skewness skewness0.068
Kurtosis Kurtosis kurtosis-0.632
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1942000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.977; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2w88a_
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.1 — Plastocyanin/azurin-like
Domain ID domain_idd2w88b_
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.1 — Plastocyanin/azurin-like
Domain ID domain_idd2w88c_
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.1 — Plastocyanin/azurin-like

CATH v4.4 (3 domains)

Domain ID domain_id2w88A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2w88B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2w88C00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins

8. Citations (1)

9. Files and Curves (10)