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- SASDG46: 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant) -

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ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDG46
Sample4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant)
  • 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant) (protein), HTPA synthase N84A, Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function / homology
Function and homology information


4-hydroxy-tetrahydrodipicolinate synthase / 4-hydroxy-tetrahydrodipicolinate synthase activity / diaminopimelate biosynthetic process / lysine biosynthetic process via diaminopimelate / cytosol
Similarity search - Function
4-hydroxy-tetrahydrodipicolinate synthase, DapA / Schiff base-forming aldolase, conserved site / Dihydrodipicolinate synthase signature 1. / Schiff base-forming aldolase, active site / Dihydrodipicolinate synthase signature 2. / DapA-like / Dihydrodipicolinate synthetase family / Dihydrodipicolinate synthetase family / Aldolase-type TIM barrel
Similarity search - Domain/homology
4-hydroxy-tetrahydrodipicolinate synthase
Similarity search - Component
Biological speciesCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (Campylobacter)
Contact author
  • Trushar Patel (University of Lethbridge, Lethbridge, AB, Canada)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #3808
Type: dummy / Software: (DAMFILT 5.0 (r9678)) / Radius of dummy atoms: 3.25 A / Chi-square value: 3.642
Search similar-shape structures of this assembly by Omokage search (details)
Model #3852
Type: dummy / Radius of dummy atoms: 1.90 A / Symmetry: P1 / Chi-square value: 3.642
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant)
Specimen concentration: 10 mg/ml
BufferName: 20 mM Tris-HCl, 150 mM NaCl / pH: 8
Entity #1919Name: HTPA synthase N84A / Type: protein
Description: 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant)
Formula weight: 32.627
Source: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
References: UniProt: Q9PPB4
Sequence: MDKNIIIGAM TALITPFKNG KVDEQSYARL IKRQIENGID AVVPVGTTGE SATLTHEEHR TCIEIAVETC KGTKVKVLAG AGSAATHEAV GLAKFAKEHG ADGILSVAPY YNKPTQQGLY EHYKAIAQSV DIPVLLYNVP GRTGCEISTD TIIKLFRDCE NIYGVKEASG ...Sequence:
MDKNIIIGAM TALITPFKNG KVDEQSYARL IKRQIENGID AVVPVGTTGE SATLTHEEHR TCIEIAVETC KGTKVKVLAG AGSAATHEAV GLAKFAKEHG ADGILSVAPY YNKPTQQGLY EHYKAIAQSV DIPVLLYNVP GRTGCEISTD TIIKLFRDCE NIYGVKEASG NIDKCVDLLA HEPRMMLISG EDAINYPILS NGGKGVISVT SNLLPDMISA LTHFALDENY KEAKKINDEL YNINKILFCE SNPIPIKTAM YLAGLIESLE FRLPLCSPSK ENFAKIEEVM KKYKIKGF

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Experimental information

BeamInstrument name: Diamond Light Source B21 / City: Didcot / 国: UK / Shape: 1 x 5 mm / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 4 mm
DetectorName: Pilatus 2M
Scan
Title: 4-hydroxy-tetrahydrodipicolinate synthase (N84A mutant)
Measurement date: Aug 2, 2017 / Exposure time: 3 sec. / Number of frames: 619 / Unit: 1/A /
MinMax
Q0.0039 0.3895
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1361 /
MinMax
Q0.012742 0.321078
P(R) point1 1361
R0 89
Result
Type of curve: sec
Comments: The models displayed in this entry represent: Top, the averaged (DAMFILT) model obtained from the spatial alignment of several individual DAMMIF models (volume and bead occupancy corrected) ...Comments: The models displayed in this entry represent: Top, the averaged (DAMFILT) model obtained from the spatial alignment of several individual DAMMIF models (volume and bead occupancy corrected) and; Bottom, and individual DAMMIF model representative and corresponding fit. Additional individual DAMMIF models (in P1 symmetry) are provided in the full entry zip archive.
ExperimentalPorod
MW109 kDa101 kDa
Volume-163 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I00.1612 4.0E-5 0.163699 9.0E-5
Radius of gyration, Rg3.24 nm0.06 3.33 nm0.03

MinMax
D-8.9
Guinier point65 155

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