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1lba

THE STRUCTURE OF BACTERIOPHAGE T7 LYSOZYME, A ZINC AMIDASE AND AN INHIBITOR OF T7 RNA POLYMERASE

Method: X-RAY DIFFRACTION Dmax: 51.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

T7 LYSOZYME

Enterobacteria phage T7

UniProt P00806

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 6–150 Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å

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 1LBA Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1ARO T7 RNA POLYMERASE COMPLEXED WITH T7 LYSOZYME Deposited 1997-08-08 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain L 1–150（150 aa）
Not recorded HG MERCURY (II) ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；pH 7.0
Resolution 2.80 Å R-free 0.309

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

View Construct and Data Evidence
UniProt name NAAA_BPT7
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 2–146； UniProt 6–150

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 1lba

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1lba
Deposition date deposition_date1993-12-22
Structure title titleTHE STRUCTURE OF BACTERIOPHAGE T7 LYSOZYME, A ZINC AMIDASE AND AN INHIBITOR OF T7 RNA POLYMERASE
Keywords keywordsHYDROLASE(ACTING ON LINEAR AMIDES); HYDROLASE(ACTING ON LINEAR AMIDES)
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_guinier15.66 Å
Radius of gyration Rg (electron density) rg_electron14.46 Å
Forward intensity I(0) i05579720.00
Molecular weight molecular_weight16385.0 kDa
Excluded volume excluded_volume20253 ų
Envelope volume envelope_volume22970 ų
Hydration-shell volume shell_volume13311 ų
Envelope diameter envelope_diameter50.1 Å
Shell Rg shell_rg20.49 Å
Envelope Rg envelope_rg14.85 Å
Shape Rg shape_rg14.44 Å
Total Rg total_rg15.64 Å
Total atoms total_atoms1151
Residues n_residues146
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 dmax51.3 Å
Rg (real space) rg_real15.56 Å
Rg uncertainty (real space) rg_real_error0.34 Å
I(0) (real space) i0_real5.5800e+06
I(0) uncertainty (real space) i0_real_error7.0200e+04
Rg (reciprocal space) rg_reciprocal15.57 Å
I(0) (reciprocal space) i0_reciprocal5580000.0000
Solution quality estimate total_estimate0.8824
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8 Å
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha899500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.996
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1lbaa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.118 — N-acetylmuramoyl-L-alanine amidase-like
Superfamily Superfamily superfamilyd.118.1 — N-acetylmuramoyl-L-alanine amidase-like
Family Family familyd.118.1.1 — N-acetylmuramoyl-L-alanine amidase-like

CATH v4.4 (1 domains)

Domain ID domain_id1lbaA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology80 — Lysozyme-like
Homologous superfamily homologous superfamily10 — Peptidoglycan recognition protein-like
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8. Citations (1)

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9. Files and Curves (10)