2mea

CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

Method: X-RAY DIFFRACTION Dmax: 65.0 Å Quality: GOOD

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

LYSOZYME

Homo sapiens

UniProt P61626

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 19–148 Mutation:I56F No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;1.5M TO 1.8M NACL, 20MM ACETATE, PH 4.5 Resolution 2.20 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 19–148 Mutation:I56F No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;1.5M TO 1.8M NACL, 20MM ACETATE, PH 4.5 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.

201 other PDB entries and 218 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYSC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–130; UniProt 19–148 Author chain B; PDBConstruct 1–130; UniProt 19–148

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 2mea

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2mea
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2mea
Deposition date deposition_date1998-05-02
Structure title titleCHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS
Keywords keywordsENZYME, HYDROLASE, O-GLYCOSYL, ALPHA + BETA, GLYCOSIDASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.15
Radius of gyration Rg (electron density) rg_electron19.13
Forward intensity I(0) i017496100.00
Molecular weight molecular_weight29486.0 kDa
Excluded volume excluded_volume36006 ų
Envelope volume envelope_volume41632 ų
Hydration-shell volume shell_volume18529 ų
Envelope diameter envelope_diameter64.4
Shell Rg shell_rg24.89
Envelope Rg envelope_rg19.22
Shape Rg shape_rg19.12
Total Rg total_rg19.93
Total atoms total_atoms2064
Residues n_residues260
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 dmax65.0
Rg (real space) rg_real20.09
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real1.7500e+07
I(0) uncertainty (real space) i0_real_error2.1990e+05
Rg (reciprocal space) rg_reciprocal20.10
I(0) (reciprocal space) i0_reciprocal17500000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.400
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha2256000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2meaa_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.2 — C-type lysozyme
Domain ID domain_idd2meab_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.2 — Lysozyme-like
Superfamily Superfamily superfamilyd.2.1 — Lysozyme-like
Family Family familyd.2.1.2 — C-type lysozyme

CATH v4.4 (2 domains)

Domain ID domain_id2meaA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10
Domain ID domain_id2meaB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (6)

9. Files and Curves (10)