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1c3u

T. MARITIMA ADENYLOSUCCINATE LYASE

Method: X-RAY DIFFRACTION Dmax: 110.3 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ADENYLOSUCCINATE LYASE

Thermotoga maritima

UniProt Q9X0I0

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–431 Chain B； UniProt 1–431 Not recorded SO4 SULFATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 9；291 K；100 mM Bicine, 5 mM AMP, 1.8 M Ammonium Sulfate, pH 9.00, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.30 Å R-free 0.230

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 1C3U Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C3C T. MARITIMA ADENYLOSUCCINATE LYASE Deposited 1999-07-27 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain not uniquely mapped Reference range not declared
Chain A 2–430（429 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.5；100 MM NAACETATE, 0.5% PEG 4000, 6% GLYCEROL, pH 4.50
Resolution 1.80 Å R-free 0.207

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

View Construct and Data Evidence
UniProt name PUR8_THEMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–431； UniProt 1–431 Author chain B； PDBConstruct 1–431； UniProt 1–431

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 1c3u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c3u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c3u
Deposition date deposition_date1999-07-28
Structure title titleT. MARITIMA ADENYLOSUCCINATE LYASE
Keywords keywordsPURINE BIOSYNTHESIS, LYASE; LYASE
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_guinier35.02 Å
Radius of gyration Rg (electron density) rg_electron34.56 Å
Forward intensity I(0) i0137559000.00
Molecular weight molecular_weight95557.0 kDa
Excluded volume excluded_volume120120 ų
Envelope volume envelope_volume155520 ų
Hydration-shell volume shell_volume38064 ų
Envelope diameter envelope_diameter111.7 Å
Shell Rg shell_rg40.56 Å
Envelope Rg envelope_rg34.07 Å
Shape Rg shape_rg34.58 Å
Total Rg total_rg34.92 Å
Total atoms total_atoms6736
Residues n_residues846
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 dmax110.3 Å
Rg (real space) rg_real34.95 Å
Rg uncertainty (real space) rg_real_error0.88 Å
I(0) (real space) i0_real1.3760e+08
I(0) uncertainty (real space) i0_real_error2.0970e+06
Rg (reciprocal space) rg_reciprocal34.99 Å
I(0) (reciprocal space) i0_reciprocal137600000.0000
Solution quality estimate total_estimate0.9114
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.1 Å
Skewness Skewness skewness0.138
Kurtosis Kurtosis kurtosis-0.717
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15040000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.958
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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) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1c3ua_
Class classa — All alpha proteins
Fold Fold folda.127 — L-aspartase-like
Superfamily Superfamily superfamilya.127.1 — L-aspartase-like
Family Family familya.127.1.1 — L-aspartase/fumarase
Domain ID domain_idd1c3ub_
Class classa — All alpha proteins
Fold Fold folda.127 — L-aspartase-like
Superfamily Superfamily superfamilya.127.1 — L-aspartase-like
Family Family familya.127.1.1 — L-aspartase/fumarase

CATH v4.4 (6 domains)

Domain ID domain_id1c3uA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology275 — Fumarase C; Chain B, domain 1
Homologous superfamily homologous superfamily10 — Fumarase/aspartase (N-terminal domain)
Domain ID domain_id1c3uA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology200 — Fumarase C; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Fumarase/aspartase (Central domain)
Domain ID domain_id1c3uA03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology40 — Ribonucleotide Reductase Protein R1; domain 1
Homologous superfamily homologous superfamily30 — Fumarase/aspartase (C-terminal domain)
Domain ID domain_id1c3uB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology275 — Fumarase C; Chain B, domain 1
Homologous superfamily homologous superfamily10 — Fumarase/aspartase (N-terminal domain)
Domain ID domain_id1c3uB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology200 — Fumarase C; Chain A, domain 2
Homologous superfamily homologous superfamily10 — Fumarase/aspartase (Central domain)
Domain ID domain_id1c3uB03
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology40 — Ribonucleotide Reductase Protein R1; domain 1
Homologous superfamily homologous superfamily30 — Fumarase/aspartase (C-terminal domain)
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8. Citations (1)

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9. Files and Curves (10)