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1c3c

T. MARITIMA ADENYLOSUCCINATE LYASE

Method: X-RAY DIFFRACTION Dmax: 110.6 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (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 not uniquely mapped； UniProt —–— Chain A； UniProt 2–430 Not recorded No other associated polymer 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

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 1C3C Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1C3U T. MARITIMA ADENYLOSUCCINATE LYASE Deposited 1999-07-28 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–431（431 aa）
Chain B 1–431（431 aa）
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

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 1–429； UniProt 2–430

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 1c3c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1c3c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1c3c
Deposition date deposition_date1999-07-27
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_guinier35.11 Å
Radius of gyration Rg (electron density) rg_electron34.64 Å
Forward intensity I(0) i0135135000.00
Molecular weight molecular_weight95419.0 kDa
Excluded volume excluded_volume120290 ų
Envelope volume envelope_volume156110 ų
Hydration-shell volume shell_volume38187 ų
Envelope diameter envelope_diameter113.0 Å
Shell Rg shell_rg40.46 Å
Envelope Rg envelope_rg34.15 Å
Shape Rg shape_rg34.67 Å
Total Rg total_rg34.98 Å
Total atoms total_atoms6734
Residues n_residues848
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 dmax110.6 Å
Rg (real space) rg_real35.04 Å
Rg uncertainty (real space) rg_real_error1.03 Å
I(0) (real space) i0_real1.3510e+08
I(0) uncertainty (real space) i0_real_error2.2220e+06
Rg (reciprocal space) rg_reciprocal35.09 Å
I(0) (reciprocal space) i0_reciprocal135100000.0000
Solution quality estimate total_estimate0.9116
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.2 Å
Skewness Skewness skewness0.146
Kurtosis Kurtosis kurtosis-0.709
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15190000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.956
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1c3ca_
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_idd1c3cb_
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_id1c3cA01
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_id1c3cA02
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_id1c3cA03
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_id1c3cB01
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_id1c3cB02
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_id1c3cB03
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)