+Open data
-Basic information
Entry | Database: PDB / ID: 1a4i | ||||||
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Title | HUMAN TETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE | ||||||
Components | METHYLENETETRAHYDROFOLATE DEHYDROGENASE / METHENYLTETRAHYDROFOLATE CYCLOHYDROLASE | ||||||
Keywords | OXIDOREDUCTASE / THF / BIFUNCTIONAL / DEHYDROGENASE / CYCLOHYDROLASE / FOLATE | ||||||
Function / homology | Function and homology information methylenetetrahydrofolate dehydrogenase [NAD(P)+] activity / serine family amino acid biosynthetic process / 10-formyltetrahydrofolate biosynthetic process / purine ribonucleotide biosynthetic process / serine family amino acid metabolic process / methylenetetrahydrofolate dehydrogenase (NAD+) activity / formate-tetrahydrofolate ligase / formate-tetrahydrofolate ligase activity / methylenetetrahydrofolate dehydrogenase (NADP+) / embryonic neurocranium morphogenesis ...methylenetetrahydrofolate dehydrogenase [NAD(P)+] activity / serine family amino acid biosynthetic process / 10-formyltetrahydrofolate biosynthetic process / purine ribonucleotide biosynthetic process / serine family amino acid metabolic process / methylenetetrahydrofolate dehydrogenase (NAD+) activity / formate-tetrahydrofolate ligase / formate-tetrahydrofolate ligase activity / methylenetetrahydrofolate dehydrogenase (NADP+) / embryonic neurocranium morphogenesis / methenyltetrahydrofolate cyclohydrolase / methenyltetrahydrofolate cyclohydrolase activity / embryonic viscerocranium morphogenesis / methylenetetrahydrofolate dehydrogenase (NADP+) activity / methionine metabolic process / somite development / Metabolism of folate and pterines / methionine biosynthetic process / transsulfuration / neutrophil homeostasis / purine nucleotide biosynthetic process / tetrahydrofolate interconversion / neural tube closure / one-carbon metabolic process / heart development / mitochondrion / extracellular exosome / ATP binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD SELENOMET / Resolution: 1.5 Å | ||||||
Authors | Allaire, M. / Li, Y. / Mackenzie, R.E. / Cygler, M. | ||||||
Citation | Journal: Structure / Year: 1998 Title: The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution. Authors: Allaire, M. / Li, Y. / MacKenzie, R.E. / Cygler, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a4i.cif.gz | 130.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a4i.ent.gz | 101.8 KB | Display | PDB format |
PDBx/mmJSON format | 1a4i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1a4i_validation.pdf.gz | 956.5 KB | Display | wwPDB validaton report |
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Full document | 1a4i_full_validation.pdf.gz | 968.2 KB | Display | |
Data in XML | 1a4i_validation.xml.gz | 28.2 KB | Display | |
Data in CIF | 1a4i_validation.cif.gz | 40.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a4/1a4i ftp://data.pdbj.org/pub/pdb/validation_reports/a4/1a4i | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-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: (-0.993999, -0.109179, 0.006835), Vector: |
-Components
#1: Protein | Mass: 32650.545 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cellular location: CYTOPLASM / Production host: Escherichia coli (E. coli) References: UniProt: P11586, methylenetetrahydrofolate dehydrogenase (NADP+), methenyltetrahydrofolate cyclohydrolase #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 44 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.5 / Details: pH 5.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F2 / Wavelength: 0.918 |
Detector | Type: PRINCETON 2K / Detector: CCD / Date: Oct 1, 1996 / Details: MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.918 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.5 Å / Num. obs: 75578 / % possible obs: 90 % / Redundancy: 10 % / Biso Wilson estimate: 16.3 Å2 / Rmerge(I) obs: 0.068 |
Reflection | *PLUS Num. measured all: 753128 |
-Processing
Software |
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Refinement | Method to determine structure: MAD SELENOMET / Resolution: 1.5→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 Details: DISORDERED RESIDUES (A241-A250,A297-A301,B297-B301) AND DISORDERED SIDE CHAINS (A83,A251,A292,A296,B296), BAD ELECTRON DENSITY (A142).
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Displacement parameters | Biso mean: 19.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.199 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |