1g27

CRYSTAL STRUCTURE OF E.COLI POLYPEPTIDE DEFORMYLASE COMPLEXED WITH THE INHIBITOR BB-3497

Method: X-RAY DIFFRACTION Dmax: 91.4 Å Quality: GOOD

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

POLYPEPTIDE 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 1–168 Not recorded NI NICKEL (II) ION × 1 BB1 2-[(FORMYL-HYDROXY-AMINO)-METHYL]-HEXANOIC ACID (1-DIMETHYLCARBAMOYL-2,2-DIMETHYL-PROPYL)-AMIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;290 K;10mg/ml PDF, 20mM BB-3497, 25% PEG 4000, 0.1M sodium citrate, 0.2M ammonium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP at 290K Resolution 2.10 Å R-free 0.270
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–168 Not recorded NI NICKEL (II) ION × 1 BB1 2-[(FORMYL-HYDROXY-AMINO)-METHYL]-HEXANOIC ACID (1-DIMETHYLCARBAMOYL-2,2-DIMETHYL-PROPYL)-AMIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;290 K;10mg/ml PDF, 20mM BB-3497, 25% PEG 4000, 0.1M sodium citrate, 0.2M ammonium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP at 290K Resolution 2.10 Å R-free 0.270
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–168 Not recorded NI NICKEL (II) ION × 1 BB1 2-[(FORMYL-HYDROXY-AMINO)-METHYL]-HEXANOIC ACID (1-DIMETHYLCARBAMOYL-2,2-DIMETHYL-PROPYL)-AMIDE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;290 K;10mg/ml PDF, 20mM BB-3497, 25% PEG 4000, 0.1M sodium citrate, 0.2M ammonium acetate, pH 5.6, VAPOR DIFFUSION, HANGING DROP at 290K Resolution 2.10 Å R-free 0.270

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 1–168 Author chain B; PDBConstruct 1–168; UniProt 1–168 Author chain C; PDBConstruct 1–168; UniProt 1–168

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 1g27

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1g27
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1g27
Deposition date deposition_date2000-10-17
Structure title titleCRYSTAL STRUCTURE OF E.COLI POLYPEPTIDE DEFORMYLASE COMPLEXED WITH THE INHIBITOR BB-3497
Keywords keywordsBB-3497, inhibition, Polypeptide deformylase, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.60
Radius of gyration Rg (electron density) rg_electron28.08
Forward intensity I(0) i053479900.00
Molecular weight molecular_weight57398.0 kDa
Excluded volume excluded_volume72187 ų
Envelope volume envelope_volume92690 ų
Hydration-shell volume shell_volume28177 ų
Envelope diameter envelope_diameter95.3
Shell Rg shell_rg34.43
Envelope Rg envelope_rg27.80
Shape Rg shape_rg28.08
Total Rg total_rg28.73
Total atoms total_atoms4017
Residues n_residues492
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 dmax91.4
Rg (real space) rg_real28.63
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real5.3480e+07
I(0) uncertainty (real space) i0_real_error7.3390e+05
Rg (reciprocal space) rg_reciprocal28.62
I(0) (reciprocal space) i0_reciprocal53480000.0000
Solution quality estimate total_estimate0.8921
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.6
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.426
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10210000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.953; Smooth: 0.814

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_idd1g27a_
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_idd1g27b_
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_idd1g27c_
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_id1g27A00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology45 — Peptide Deformylase
Homologous superfamily homologous superfamily10 — Peptide deformylase
Domain ID domain_id1g27B00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology45 — Peptide Deformylase
Homologous superfamily homologous superfamily10 — Peptide deformylase
Domain ID domain_id1g27C00
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)