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- PDB-1qj3: Crystal structure of 7,8-diaminopelargonic acid synthase in compl... -
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Basic information
Entry | Database: PDB / ID: 1qj3 | ||||||
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Title | Crystal structure of 7,8-diaminopelargonic acid synthase in complex with 7-keto-8-aminopelargonic acid | ||||||
![]() | 7,8-DIAMINOPELARGONIC ACID SYNTHASE | ||||||
![]() | TRANSFERASE / AMINOTRANSFERASE / PYRIDOXAL-5'-PHOSPHATE / BIOTIN BIOSYNTHESIS | ||||||
Function / homology | ![]() adenosylmethionine-8-amino-7-oxononanoate transaminase / adenosylmethionine-8-amino-7-oxononanoate transaminase activity / biotin biosynthetic process / pyridoxal phosphate binding / protein homodimerization activity / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Kaeck, H. / Sandmark, J. / Gibson, K.J. / Lindqvist, Y. / Schneider, G. | ||||||
![]() | ![]() Title: Crystal Structure of Diaminopelargonic Acid Synthase; Evolutionary Relationships between Pyridoxal-5'-Phosphate Dependent Enzymes Authors: Kack, H. / Sandmark, J. / Gibson, K.J. / Schneider, G. / Lindqvist, Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 168.8 KB | Display | ![]() |
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PDB format | ![]() | 139.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.99995, 0.01019, 0.0007), Vector: |
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Components
#1: Protein | Mass: 47310.391 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P12995, adenosylmethionine-8-amino-7-oxononanoate transaminase #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | Nonpolymer details | PYRIDOXAL-5'-PHOSPHATE IS BOUND TO LYS 274 IN BOTH CHAINS | Sequence details | FROM THE ELECTRON DENSITY TRP14 IS REINTERPRE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 30 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / pH: 7.5 Details: 25% PEG-4000, 20% MPD, 100MM HEPES PH7.5, 5MM KAPA (7-KETO-8-AMINOPELARGONIC ACID), 20 DEGREES C, MICROSEEDING., pH 7.50 | ||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.3 / Method: vapor diffusionDetails: drop consists of equal volume of protein and precipitant solutions | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 15, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→20 Å / Num. obs: 21479 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 5.8 % / Biso Wilson estimate: 42.6 Å2 / Rsym value: 0.104 / Net I/σ(I): 17.6 |
Reflection shell | Resolution: 2.7→2.82 Å / Mean I/σ(I) obs: 5.4 / Rsym value: 0.326 / % possible all: 99.7 |
Reflection | *PLUS Num. measured all: 124908 / Rmerge(I) obs: 0.104 |
Reflection shell | *PLUS % possible obs: 99.7 % / Rmerge(I) obs: 0.326 |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 2.7→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: DUE TO DISORDERED MAINCHAIN THE FOLLOWING RESIDUES WERE REMOVED FROM THE MODEL OF CHAIN A: SER 160, MET 161, HIS 162, SER 163, LEU 164, TRP 165, LYS 166, GLY 167, TYR 168, ASP 183, GLY 300, ...Details: DUE TO DISORDERED MAINCHAIN THE FOLLOWING RESIDUES WERE REMOVED FROM THE MODEL OF CHAIN A: SER 160, MET 161, HIS 162, SER 163, LEU 164, TRP 165, LYS 166, GLY 167, TYR 168, ASP 183, GLY 300, ALA 301, GLN 429 DUE TO DISORDERED MAINCHAIN THE FOLLOWING RESIDUES WERE REMOVED FROM THE MODEL OF CHAIN B: SER 160, MET 161, HIS 162, SER 163, LEU 164, TRP 165, LYS 166, GLY 167, TYR 168, ASP 183, GLY 184, GLY 300, ALA 301, GLN 429
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Displacement parameters | Biso mean: 51.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→20 Å
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Refine LS restraints |
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