1ojm

SPECIFICITY AND MECHANISM OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE: COMPLEX WITH UNSULPHATED CHONDROITIN DISACCHARIDE

Method: X-RAY DIFFRACTION Dmax: 92.1 Å Quality: GOOD

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

HYALURONATE LYASE

STREPTOCOCCUS PNEUMONIAE

UniProt Q54873

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 291–1009 Fragment:HYALURONATE LYASE, RESIDUES 287-1009 4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose × 1 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;3.5M AMMONIUM SULFATE, 200MM SODIUM CACODYLATE, PH 6.0 Resolution 1.78 Å R-free 0.224

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.

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HYSA_STRPN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–723; UniProt 291–1009

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 1ojm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ojm
Deposition date deposition_date2003-07-11
Structure title titleSPECIFICITY AND MECHANISM OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE: COMPLEX WITH UNSULPHATED CHONDROITIN DISACCHARIDE
Keywords keywordsLYASE, PROTEIN-CARBOHYDRATE COMPLEX; LYASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.34
Radius of gyration Rg (electron density) rg_electron27.52
Forward intensity I(0) i0115034000.00
Molecular weight molecular_weight82968.0 kDa
Excluded volume excluded_volume102950 ų
Envelope volume envelope_volume121480 ų
Hydration-shell volume shell_volume36386 ų
Envelope diameter envelope_diameter96.2
Shell Rg shell_rg35.48
Envelope Rg envelope_rg27.68
Shape Rg shape_rg27.50
Total Rg total_rg28.32
Total atoms total_atoms5837
Residues n_residues722
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 dmax92.1
Rg (real space) rg_real28.32
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.1500e+08
I(0) uncertainty (real space) i0_real_error1.5070e+06
Rg (reciprocal space) rg_reciprocal28.33
I(0) (reciprocal space) i0_reciprocal115000000.0000
Solution quality estimate total_estimate0.8882
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.9
Skewness Skewness skewness0.370
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha30530000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.857; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1ojma1
Class classa — All alpha proteins
Fold Fold folda.102 — alpha/alpha toroid
Superfamily Superfamily superfamilya.102.3 — Chondroitin AC/alginate lyase
Family Family familya.102.3.2 — Hyaluronate lyase-like catalytic, N-terminal domain
Domain ID domain_idd1ojma2
Class classb — All beta proteins
Fold Fold foldb.24 — Hyaluronate lyase-like, C-terminal domain
Superfamily Superfamily superfamilyb.24.1 — Hyaluronate lyase-like, C-terminal domain
Family Family familyb.24.1.1 — Hyaluronate lyase-like, C-terminal domain
Domain ID domain_idd1ojma3
Class classb — All beta proteins
Fold Fold foldb.30 — Supersandwich
Superfamily Superfamily superfamilyb.30.5 — Galactose mutarotase-like
Family Family familyb.30.5.2 — Hyaluronate lyase-like, central domain
Domain ID domain_idd1ojma4
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (3 domains)

Domain ID domain_id1ojmA01
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily10
Domain ID domain_id1ojmA02
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily100 — Chondroitin AC/alginate lyase
Domain ID domain_id1ojmA03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology220 — Chondroitinase Ac; Chain A, domain 3
Homologous superfamily homologous superfamily10 — Polysaccharide lyase family 8-like, C-terminal

8. Citations (2)

9. Files and Curves (10)