2gpw

Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.

Method: X-RAY DIFFRACTION Dmax: 153.7 Å Quality: GOOD

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

Biotin carboxylase

Escherichia coli

UniProt P24182

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–449 Mutation:F363A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;294 K;0.1 M Bis-Tris (pH 7.5), 100 mM NaCl, 200 mM trimethylamine N-oxide, 8% (v/v) PEG2000 MME, 4% (v/v) glycerol, 5 mM magnesium chloride, and 2.5 mM DTT, VAPOR DIFFUSION, temperature 294K Resolution 2.20 Å R-free 0.250
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–449 Mutation:F363A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;294 K;0.1 M Bis-Tris (pH 7.5), 100 mM NaCl, 200 mM trimethylamine N-oxide, 8% (v/v) PEG2000 MME, 4% (v/v) glycerol, 5 mM magnesium chloride, and 2.5 mM DTT, VAPOR DIFFUSION, temperature 294K Resolution 2.20 Å R-free 0.250
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–449 Mutation:F363A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;294 K;0.1 M Bis-Tris (pH 7.5), 100 mM NaCl, 200 mM trimethylamine N-oxide, 8% (v/v) PEG2000 MME, 4% (v/v) glycerol, 5 mM magnesium chloride, and 2.5 mM DTT, VAPOR DIFFUSION, temperature 294K Resolution 2.20 Å R-free 0.250
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–449 Mutation:F363A No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;294 K;0.1 M Bis-Tris (pH 7.5), 100 mM NaCl, 200 mM trimethylamine N-oxide, 8% (v/v) PEG2000 MME, 4% (v/v) glycerol, 5 mM magnesium chloride, and 2.5 mM DTT, VAPOR DIFFUSION, temperature 294K Resolution 2.20 Å R-free 0.250

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.

29 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACCC_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 21–469; UniProt 1–449 Author chain B; PDBConstruct 21–469; UniProt 1–449 Author chain C; PDBConstruct 21–469; UniProt 1–449 Author chain D; PDBConstruct 21–469; UniProt 1–449

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 2gpw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2gpw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2gpw
Deposition date deposition_date2006-04-18
Structure title titleCrystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.
Keywords keywordsATP-grasp, carboxylase, biotin-dependent, fatty acid synthesis, dimer-interface mutant, Ligase; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.84
Radius of gyration Rg (electron density) rg_electron44.60
Forward intensity I(0) i0574064000.00
Molecular weight molecular_weight195680.0 kDa
Excluded volume excluded_volume244580 ų
Envelope volume envelope_volume327380 ų
Hydration-shell volume shell_volume62372 ų
Envelope diameter envelope_diameter157.9
Shell Rg shell_rg47.81
Envelope Rg envelope_rg44.44
Shape Rg shape_rg44.56
Total Rg total_rg44.86
Total atoms total_atoms13731
Residues n_residues1780
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 dmax153.7
Rg (real space) rg_real44.99
Rg uncertainty (real space) rg_real_error2.07
I(0) (real space) i0_real5.7410e+08
I(0) uncertainty (real space) i0_real_error1.1700e+07
Rg (reciprocal space) rg_reciprocal44.84
I(0) (reciprocal space) i0_reciprocal574000000.0000
Solution quality estimate total_estimate0.8599
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.9
Skewness Skewness skewness0.389
Kurtosis Kurtosis kurtosis-0.386
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha74880000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.722

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 28 domains

SCOP 2.08 (16 domains)

Domain ID domain_idd2gpwa1
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.2 — Rudiment single hybrid motif
Family Family familyb.84.2.1 — BC C-terminal domain-like
Domain ID domain_idd2gpwa2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.30 — PreATP-grasp domain
Superfamily Superfamily superfamilyc.30.1 — PreATP-grasp domain
Family Family familyc.30.1.1 — BC N-terminal domain-like
Domain ID domain_idd2gpwa3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.142 — ATP-grasp
Superfamily Superfamily superfamilyd.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family familyd.142.1.2 — BC ATP-binding domain-like
Domain ID domain_idd2gpwa4
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2gpwb1
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.2 — Rudiment single hybrid motif
Family Family familyb.84.2.1 — BC C-terminal domain-like
Domain ID domain_idd2gpwb2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.30 — PreATP-grasp domain
Superfamily Superfamily superfamilyc.30.1 — PreATP-grasp domain
Family Family familyc.30.1.1 — BC N-terminal domain-like
Domain ID domain_idd2gpwb3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.142 — ATP-grasp
Superfamily Superfamily superfamilyd.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family familyd.142.1.2 — BC ATP-binding domain-like
Domain ID domain_idd2gpwb4
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2gpwc1
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.2 — Rudiment single hybrid motif
Family Family familyb.84.2.1 — BC C-terminal domain-like
Domain ID domain_idd2gpwc2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.30 — PreATP-grasp domain
Superfamily Superfamily superfamilyc.30.1 — PreATP-grasp domain
Family Family familyc.30.1.1 — BC N-terminal domain-like
Domain ID domain_idd2gpwc3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.142 — ATP-grasp
Superfamily Superfamily superfamilyd.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family familyd.142.1.2 — BC ATP-binding domain-like
Domain ID domain_idd2gpwc4
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2gpwd1
Class classb — All beta proteins
Fold Fold foldb.84 — Barrel-sandwich hybrid
Superfamily Superfamily superfamilyb.84.2 — Rudiment single hybrid motif
Family Family familyb.84.2.1 — BC C-terminal domain-like
Domain ID domain_idd2gpwd2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.30 — PreATP-grasp domain
Superfamily Superfamily superfamilyc.30.1 — PreATP-grasp domain
Family Family familyc.30.1.1 — BC N-terminal domain-like
Domain ID domain_idd2gpwd3
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.142 — ATP-grasp
Superfamily Superfamily superfamilyd.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family familyd.142.1.2 — BC ATP-binding domain-like
Domain ID domain_idd2gpwd4
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (12 domains)

Domain ID domain_id2gpwA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily20
Domain ID domain_id2gpwA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, B domain
Domain ID domain_id2gpwA03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, A domain
Domain ID domain_id2gpwB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily20
Domain ID domain_id2gpwB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, B domain
Domain ID domain_id2gpwB03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, A domain
Domain ID domain_id2gpwC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily20
Domain ID domain_id2gpwC02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, B domain
Domain ID domain_id2gpwC03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, A domain
Domain ID domain_id2gpwD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily20
Domain ID domain_id2gpwD02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, B domain
Domain ID domain_id2gpwD03
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, A domain

8. Citations (1)

9. Files and Curves (10)