2gu4

E. coli methionine aminopeptidase in complex with NleP, 1: 0.5, di-metalated

Method: X-RAY DIFFRACTION Dmax: 86.7 Å Quality: GOOD

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

Methionine aminopeptidase

Escherichia coli

UniProt P0AE18

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 2–264 Not recorded MN MANGANESE (II) ION × 2 NA SODIUM ION × 1 NLP (1-AMINO-PENTYL)-PHOSPHONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;291 K;15% PEG 20000, 0.1 M MES (pH 6.5) , VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.80 Å R-free 0.227
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–264 Not recorded MN MANGANESE (II) ION × 2 NA SODIUM ION × 1 NLP (1-AMINO-PENTYL)-PHOSPHONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;291 K;15% PEG 20000, 0.1 M MES (pH 6.5) , VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.80 Å R-free 0.227

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.

28 other PDB entries and 33 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 1–263; UniProt 2–264 Author chain B; PDBConstruct 1–263; UniProt 2–264

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 2gu4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2gu4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2gu4
Deposition date deposition_date2006-04-28
Structure title titleE. coli methionine aminopeptidase in complex with NleP, 1: 0.5, di-metalated
Keywords keywordsMono-metalated, mononuclear, Mn(II)-form, hydrolase, enzyme-inhibitor complex, metalloenzyme; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.49
Radius of gyration Rg (electron density) rg_electron25.84
Forward intensity I(0) i057624500.00
Molecular weight molecular_weight58615.0 kDa
Excluded volume excluded_volume73171 ų
Envelope volume envelope_volume86047 ų
Hydration-shell volume shell_volume27849 ų
Envelope diameter envelope_diameter96.3
Shell Rg shell_rg32.95
Envelope Rg envelope_rg25.83
Shape Rg shape_rg25.85
Total Rg total_rg26.56
Total atoms total_atoms4088
Residues n_residues522
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 dmax86.7
Rg (real space) rg_real26.52
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real5.7620e+07
I(0) uncertainty (real space) i0_real_error9.7450e+05
Rg (reciprocal space) rg_reciprocal26.52
I(0) (reciprocal space) i0_reciprocal57620000.0000
Solution quality estimate total_estimate0.8103
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary85.3
Skewness Skewness skewness0.344
Kurtosis Kurtosis kurtosis-0.474
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19240000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2gu4a_
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
Domain ID domain_idd2gu4b_
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 (2 domains)

Domain ID domain_id2gu4A00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology230 — Creatine Amidinohydrolase
Homologous superfamily homologous superfamily10 — Creatinase/methionine aminopeptidase superfamily
Domain ID domain_id2gu4B00
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)