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1bue

NMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE

Method: X-RAY DIFFRACTION Dmax: 63.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (IMIPENEM-HYDROLYSING BETA-LACTAMASE)

Enterobacter cloacae

UniProt P52663

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 28–292 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 5.25；INITIAL PROTEIN CONCENTRATION WAS 2.0 G/L EQUILIBRATED AGAINST 0.200 M MES PH 5.25, 20% (W/V)PEG 1500, 6% (V/V) N-PROPANOL AT 295K. Resolution 1.64 Å R-free 0.214

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.

Other PDB Difference from Current Entry 1BUE Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BUL 6ALPHA-(HYDROXYPROPYL)PENICILLANATE ACYLATED ON NMC-A BETA-LACTAMASE FROM ENTEROBACTER CLOACAE Deposited 1998-09-04 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–292（265 aa）
Not recorded AP3 2-(1-CARBOXY-2-HYDROXY-2-METHYL-PROPYL)-5,5-DIMETHYL-THIAZOLIDINE-4-CARBOXYLIC ACID × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 3 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；20% (W/V)PEG 1500, 0.200 M MES PH 5.25, 6% (V/V) N-PROPANOL, pH 7.5
Resolution 1.89 Å R-free 0.257

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BLAN_ENTCL
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–265； UniProt 28–292

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 1bue

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bue
Deposition date deposition_date1998-09-03
Structure title titleNMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE
Keywords keywordsHYDROLASE, ANTIBIOTIC RESISTANCE, CLASS A CARBAPENEMASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.07 Å
Radius of gyration Rg (electron density) rg_electron17.87 Å
Forward intensity I(0) i015408600.00
Molecular weight molecular_weight28730.0 kDa
Excluded volume excluded_volume35578 ų
Envelope volume envelope_volume40233 ų
Hydration-shell volume shell_volume18670 ų
Envelope diameter envelope_diameter65.3 Å
Shell Rg shell_rg24.34 Å
Envelope Rg envelope_rg18.27 Å
Shape Rg shape_rg17.87 Å
Total Rg total_rg18.78 Å
Total atoms total_atoms2024
Residues n_residues265
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax63.9 Å
Rg (real space) rg_real18.99 Å
Rg uncertainty (real space) rg_real_error0.35 Å
I(0) (real space) i0_real1.5410e+07
I(0) uncertainty (real space) i0_real_error1.8310e+05
Rg (reciprocal space) rg_reciprocal19.00 Å
I(0) (reciprocal space) i0_reciprocal15410000.0000
Solution quality estimate total_estimate0.8751
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.0 Å
Skewness Skewness skewness0.265
Kurtosis Kurtosis kurtosis-0.264
Angular range angular_range— – 0.4150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3851000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.796; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.985
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1buea_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.3 — beta-lactamase/transpeptidase-like
Superfamily Superfamily superfamilye.3.1 — beta-lactamase/transpeptidase-like
Family Family familye.3.1.1 — beta-Lactamase/D-ala carboxypeptidase

CATH v4.4 (1 domains)

Domain ID domain_id1bueA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology710 — Beta-lactamase
Homologous superfamily homologous superfamily10 — DD-peptidase/beta-lactamase superfamily
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8. Citations (3)

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9. Files and Curves (10)