1xnz

Crystal Structure of Mn(II) form of E. coli. Methionine Aminopeptidase in complex with 5-(2-chlorophenyl)furan-2-carboxylic acid

Method: X-RAY DIFFRACTION Dmax: 56.8 Å Quality: GOOD

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

Methionine aminopeptidase

Escherichia coli

UniProt P07906

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 1–264 Not recorded MN MANGANESE (II) ION × 2 NA SODIUM ION × 1 FCD 5-(2-CHLOROPHENYL)FURAN-2-CARBOXYLIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;292 K;15% PEG 8000, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, temperature 292K Resolution 1.52 Å R-free 0.250

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.

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

View Construct and Data Evidence
UniProt name AMPM_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–264; UniProt 1–264

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 1xnz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1xnz
Deposition date deposition_date2004-10-05
Structure title titleCrystal Structure of Mn(II) form of E. coli. Methionine Aminopeptidase in complex with 5-(2-chlorophenyl)furan-2-carboxylic acid
Keywords keywordsMethionine Aminopeptidase, complex, inhibitor, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.18
Radius of gyration Rg (electron density) rg_electron17.19
Forward intensity I(0) i015288800.00
Molecular weight molecular_weight29402.0 kDa
Excluded volume excluded_volume36761 ų
Envelope volume envelope_volume39618 ų
Hydration-shell volume shell_volume18748 ų
Envelope diameter envelope_diameter57.9
Shell Rg shell_rg23.90
Envelope Rg envelope_rg17.57
Shape Rg shape_rg17.19
Total Rg total_rg18.14
Total atoms total_atoms2052
Residues n_residues262
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 dmax56.8
Rg (real space) rg_real18.05
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real1.5290e+07
I(0) uncertainty (real space) i0_real_error1.6380e+05
Rg (reciprocal space) rg_reciprocal18.06
I(0) (reciprocal space) i0_reciprocal15290000.0000
Solution quality estimate total_estimate0.8941
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.3
Skewness Skewness skewness0.159
Kurtosis Kurtosis kurtosis-0.422
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4265000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1xnza_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.127 — Creatinase/aminopeptidase
Superfamily Superfamily superfamilyd.127.1 — Creatinase/aminopeptidase
Family Family familyd.127.1.1 — Creatinase/aminopeptidase

CATH v4.4 (1 domains)

Domain ID domain_id1xnzA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology230 — Creatine Amidinohydrolase
Homologous superfamily homologous superfamily10 — Creatinase/methionine aminopeptidase superfamily

8. Citations (1)

9. Files and Curves (10)