1amz

CHICKEN CITRATE SYNTHASE COMPLEX WITH NITROMETHYLDE-COA AND MALATE

Method: X-RAY DIFFRACTION Dmax: 72.2 Å Quality: EXCELLENT

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

CITRATE SYNTHASE

OrganismNot specified

UniProt P23007

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 3–429 Not recorded MLT D-MALATE × 2 NMX NITROMETHYLDETHIA COENZYME A × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;CRYSTALLIZED FROM 1.01M NA MALATE, PH 6.0 2 MM NITROMETHYLDETHIA COENZYME A THE CELL ANGLE BETA IS DEFINED AS THE ACUTE ANGLE FOR CONSISTENCY WITH PREVIOUS PDB ENTRIES OF CITRATE SYNTHASE IN THIS SPACE GROUP Resolution 1.80 Å

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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CISY_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–431; UniProt 3–429

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 1amz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1amz
Deposition date deposition_date1997-06-19
Structure title titleCHICKEN CITRATE SYNTHASE COMPLEX WITH NITROMETHYLDE-COA AND MALATE
Keywords keywordsOXO-ACID-LYASE, TRICARBOXYLIC ACID CYCLE, ALLOSTERIC ENZYME; OXO-ACID-LYASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.29
Radius of gyration Rg (electron density) rg_electron22.13
Forward intensity I(0) i040016000.00
Molecular weight molecular_weight49034.0 kDa
Excluded volume excluded_volume61409 ų
Envelope volume envelope_volume73072 ų
Hydration-shell volume shell_volume26933 ų
Envelope diameter envelope_diameter74.2
Shell Rg shell_rg29.76
Envelope Rg envelope_rg22.62
Shape Rg shape_rg22.11
Total Rg total_rg23.08
Total atoms total_atoms3451
Residues n_residues435
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 dmax72.2
Rg (real space) rg_real23.18
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real4.0020e+07
I(0) uncertainty (real space) i0_real_error5.2290e+05
Rg (reciprocal space) rg_reciprocal23.21
I(0) (reciprocal space) i0_reciprocal40020000.0000
Solution quality estimate total_estimate0.9030
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.8
Skewness Skewness skewness0.226
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7478000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1amza_
Class classa — All alpha proteins
Fold Fold folda.103 — Citrate synthase
Superfamily Superfamily superfamilya.103.1 — Citrate synthase
Family Family familya.103.1.1 — Citrate synthase

CATH v4.4 (2 domains)

Domain ID domain_id1amzA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology580 — Citrate Synthase; domain 1
Homologous superfamily homologous superfamily10 — Citrate Synthase, domain 1
Domain ID domain_id1amzA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology230 — Cytochrome p450-Terp; domain 2
Homologous superfamily homologous superfamily10 — Cytochrome P450-Terp, domain 2

8. Citations (5)

9. Files and Curves (10)