1cb8

CHONDROITINASE AC LYASE FROM FLAVOBACTERIUM HEPARINUM

Method: X-RAY DIFFRACTION Dmax: 97.1 Å Quality: GOOD

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

PROTEIN (CHONDROITINASE AC)

OrganismNot specified

UniProt Q59288

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 23–700 Not recorded ;methyl alpha-L-fucopyranoside-(1-4)-beta-D-xylopyranose-(1-4)-alpha-D-glucopyranuronic acid-(1-2)-[alpha-L-rhamnopyranose-(1-4)]alpha-D-mannopyranose ; × 1 CA CALCIUM ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;CRYSTALLIZATION CONDITIONS: PEG-MME 2K 17% AMMONIUM ACETATE 80MM PH 6.5 0.4M SODIUM ACETATE Resolution 1.90 Å R-free 0.260

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHAC_SPHHE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–678; UniProt 23–700

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 1cb8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cb8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cb8
Deposition date deposition_date1999-03-02
Structure title titleCHONDROITINASE AC LYASE FROM FLAVOBACTERIUM HEPARINUM
Keywords keywordsLYASE, CHONDROITIN DEGRADATION; LYASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.18
Radius of gyration Rg (electron density) rg_electron27.56
Forward intensity I(0) i092962500.00
Molecular weight molecular_weight76998.0 kDa
Excluded volume excluded_volume96709 ų
Envelope volume envelope_volume114860 ų
Hydration-shell volume shell_volume34859 ų
Envelope diameter envelope_diameter103.8
Shell Rg shell_rg35.00
Envelope Rg envelope_rg27.85
Shape Rg shape_rg27.51
Total Rg total_rg28.41
Total atoms total_atoms5443
Residues n_residues675
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 dmax97.1
Rg (real space) rg_real28.24
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real9.2960e+07
I(0) uncertainty (real space) i0_real_error1.3750e+06
Rg (reciprocal space) rg_reciprocal28.22
I(0) (reciprocal space) i0_reciprocal92960000.0000
Solution quality estimate total_estimate0.8598
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.446
Kurtosis Kurtosis kurtosis-0.194
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17790000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.757; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1cb8a1
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_idd1cb8a2
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_idd1cb8a3
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

CATH v4.4 (3 domains)

Domain ID domain_id1cb8A01
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily100 — Chondroitin AC/alginate lyase
Domain ID domain_id1cb8A02
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology98 — Beta-galactosidase; Chain A, domain 5
Homologous superfamily homologous superfamily10
Domain ID domain_id1cb8A03
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)