5hmv

Re refinement of 4mwk.

Method: X-RAY DIFFRACTION Dmax: 49.7 Å Quality: GOOD

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

Lysozyme C

OrganismNot specified

UniProt P00698

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 19–146 Not recorded DMS DIMETHYL SULFOXIDE × 3 NO3 NITRATE ION × 7 PT PLATINUM (II) ION × 7 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;pH 4.7;294 K;40MG HEWL CO-CRYSTALLISED WITH 2.6MG CISPLATIN, WITH THE PLATINUM COMPOUNDS BEING IN A 3-FOLD MOLAR EXCESS TO THE PROTEIN. 462.5 MicroL OF A 0.02M NAAC SOLUTION ALONG WITH 462.5 MicroL OF A 0.5M NANO3 SOLUTION WAS USED WITH 75 MicroL DMSO ADDED, BATCH, PH 4.7, EVAPORATION, TEMPERATURE 294K Resolution 0.98 Å R-free 0.147

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.

1320 other PDB entries and 1450 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYSC_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–128; UniProt 19–146

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 5hmv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5hmv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5hmv
Deposition date deposition_date2016-01-17
Structure title titleRe refinement of 4mwk.
Keywords keywordsStructural dynamics cisplatin histidine protein, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.29
Radius of gyration Rg (electron density) rg_electron14.14
Forward intensity I(0) i07900710.00
Molecular weight molecular_weight16296.0 kDa
Excluded volume excluded_volume18074 ų
Envelope volume envelope_volume20433 ų
Hydration-shell volume shell_volume12347 ų
Envelope diameter envelope_diameter51.2
Shell Rg shell_rg19.84
Envelope Rg envelope_rg14.48
Shape Rg shape_rg14.06
Total Rg total_rg15.16
Total atoms total_atoms1041
Residues n_residues128
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 dmax49.7
Rg (real space) rg_real15.19
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real7.9010e+06
I(0) uncertainty (real space) i0_real_error8.2660e+04
Rg (reciprocal space) rg_reciprocal15.20
I(0) (reciprocal space) i0_reciprocal7901000.0000
Solution quality estimate total_estimate0.8680
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.1
Skewness Skewness skewness0.060
Kurtosis Kurtosis kurtosis-0.228
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.773; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.965

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5hmva_
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 (1 domains)

Domain ID domain_id5hmvA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (2)

9. Files and Curves (10)