4al2

peptide deformylase (Ni-form) with hydrosulfide

Method: X-RAY DIFFRACTION Dmax: 83.6 Å Quality: EXCELLENT

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

PEPTIDE DEFORMYLASE

ESCHERICHIA COLI

UniProt P0A6K3

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–169 Not recorded NI NICKEL (II) ION × 1 H2S HYDROSULFURIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;293 K;25% PEG 4000, 200 MM NAOAC PH 4.6, 293 K, INCUBATED IN H2S ATMOSPHERE EQUILIBRATED WITH 50 MM NA2S AT PH 4.6 Resolution 2.60 Å R-free 0.298
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–169 Not recorded NI NICKEL (II) ION × 1 H2S HYDROSULFURIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;293 K;25% PEG 4000, 200 MM NAOAC PH 4.6, 293 K, INCUBATED IN H2S ATMOSPHERE EQUILIBRATED WITH 50 MM NA2S AT PH 4.6 Resolution 2.60 Å R-free 0.298
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 2–169 Not recorded NI NICKEL (II) ION × 1 H2S HYDROSULFURIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;293 K;25% PEG 4000, 200 MM NAOAC PH 4.6, 293 K, INCUBATED IN H2S ATMOSPHERE EQUILIBRATED WITH 50 MM NA2S AT PH 4.6 Resolution 2.60 Å R-free 0.298

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.

30 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DEF_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–168; UniProt 2–169 Author chain B; PDBConstruct 1–168; UniProt 2–169 Author chain C; PDBConstruct 1–168; UniProt 2–169

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 4al2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4al2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4al2
Deposition date deposition_date2012-02-29
Structure title titlepeptide deformylase (Ni-form) with hydrosulfide
Keywords keywordsHYDROLASE, OXIDATION-REDUCTION; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.95
Radius of gyration Rg (electron density) rg_electron25.90
Forward intensity I(0) i053255700.00
Molecular weight molecular_weight56326.0 kDa
Excluded volume excluded_volume70607 ų
Envelope volume envelope_volume89949 ų
Hydration-shell volume shell_volume29105 ų
Envelope diameter envelope_diameter85.0
Shell Rg shell_rg33.05
Envelope Rg envelope_rg25.68
Shape Rg shape_rg25.93
Total Rg total_rg26.62
Total atoms total_atoms3938
Residues n_residues491
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 dmax83.6
Rg (real space) rg_real26.85
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real5.3260e+07
I(0) uncertainty (real space) i0_real_error7.5220e+05
Rg (reciprocal space) rg_reciprocal26.88
I(0) (reciprocal space) i0_reciprocal53260000.0000
Solution quality estimate total_estimate0.9083
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary82.2
Skewness Skewness skewness0.187
Kurtosis Kurtosis kurtosis-0.531
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11680000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd4al2a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.167 — Peptide deformylase
Superfamily Superfamily superfamilyd.167.1 — Peptide deformylase
Family Family familyd.167.1.1 — Peptide deformylase
Domain ID domain_idd4al2b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.167 — Peptide deformylase
Superfamily Superfamily superfamilyd.167.1 — Peptide deformylase
Family Family familyd.167.1.1 — Peptide deformylase
Domain ID domain_idd4al2c_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.167 — Peptide deformylase
Superfamily Superfamily superfamilyd.167.1 — Peptide deformylase
Family Family familyd.167.1.1 — Peptide deformylase

CATH v4.4 (3 domains)

Domain ID domain_id4al2A00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology45 — Peptide Deformylase
Homologous superfamily homologous superfamily10 — Peptide deformylase
Domain ID domain_id4al2B00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology45 — Peptide Deformylase
Homologous superfamily homologous superfamily10 — Peptide deformylase
Domain ID domain_id4al2C00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology45 — Peptide Deformylase
Homologous superfamily homologous superfamily10 — Peptide deformylase

8. Citations (1)

9. Files and Curves (10)