1qdr

2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35

Method: X-RAY DIFFRACTION Dmax: 82.3 Å Quality: REASONABLE

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

LYTIC MUREIN TRANSGLYCOSYLASE B

Escherichia coli

UniProt P41052

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 40–361 Fragment:SLT35 Mutation:L40M, L41V NA SODIUM ION × 1 BCN BICINE × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;295 K;PEG 20K, BICINE-NAOH, ISOPROPANOL, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.10 Å R-free 0.210

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLTB_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–322; UniProt 40–361

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 1qdr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1qdr
Deposition date deposition_date1999-07-10
Structure title title2.1 A RESOLUTION STRUCTURE OF ESCHERICHIA COLI LYTIC TRANSGLYCOSYLASE SLT35
Keywords keywordsALPHA-HELICAL PROTEIN WITH AN FIVE-STRANDED ANTIPARALLEL BETA-SHEET, GLYCOSYL TRANSFERASE, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.25
Radius of gyration Rg (electron density) rg_electron22.27
Forward intensity I(0) i021466600.00
Molecular weight molecular_weight35267.0 kDa
Excluded volume excluded_volume44023 ų
Envelope volume envelope_volume52743 ų
Hydration-shell volume shell_volume20568 ų
Envelope diameter envelope_diameter83.8
Shell Rg shell_rg28.11
Envelope Rg envelope_rg22.72
Shape Rg shape_rg22.24
Total Rg total_rg23.09
Total atoms total_atoms2492
Residues n_residues312
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 dmax82.3
Rg (real space) rg_real23.33
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real2.1470e+07
I(0) uncertainty (real space) i0_real_error3.4710e+05
Rg (reciprocal space) rg_reciprocal23.31
I(0) (reciprocal space) i0_reciprocal21470000.0000
Solution quality estimate total_estimate0.6489
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.459
Kurtosis Kurtosis kurtosis-0.177
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4581000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.753; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.871; Smooth: 0.956

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1qdra_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.6 — Bacterial muramidase, catalytic domain

CATH v4.4 (2 domains)

Domain ID domain_id1qdrA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology8 — Helicase, Ruva Protein; domain 3
Homologous superfamily homologous superfamily350 — Bacterial muramidase
Domain ID domain_id1qdrA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (3)

9. Files and Curves (10)