- PDB-2yii: Manipulating the regioselectivity of phenylalanine aminomutase: n... -
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ID or keywords:
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Basic information
Entry
Database: PDB / ID: 2yii
Title
Manipulating the regioselectivity of phenylalanine aminomutase: new insights into the reaction mechanism of MIO-dependent enzymes from structure-guided directed evolution
Components
PHENYLALANINE AMMONIA-LYASE
Keywords
LYASE
Function / homology
Function and homology information
phenylalanine aminomutase (L-beta-phenylalanine forming) / intramolecular aminotransferase activity / paclitaxel biosynthetic process / phenylalanine ammonia-lyase / L-phenylalanine metabolic process / cinnamic acid biosynthetic process / alkaloid biosynthetic process / phenylalanine ammonia-lyase activity / L-phenylalanine catabolic process / protein homotetramerization / cytoplasm Similarity search - Function
Mass: 77553.633 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: THIOESTER BOND BETWEEN THE MDO PROSTHETIC GROUP AND A MOLECULE OF BETA-MERCAPTOETHANOL, DISULFIDE BRIDGE BETWEEN RESIDUE C89 AND A BETA-MERCAPTOETHANOL MOLECULE, COVALENT BOND BETWEEN MDO 175 AND RESIDUE D178 Source: (gene. exp.) TAXUS WALLICHIANA VAR. CHINENSIS (Chinese yew) Plasmid: PBAD / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): K-12 / Variant (production host): TOP10 References: UniProt: Q68G84, EC: 5.4.3.-, phenylalanine ammonia-lyase
Resolution: 2.18→98.31 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.932 / SU B: 5.134 / SU ML: 0.132 / Cross valid method: THROUGHOUT / ESU R: 0.254 / ESU R Free: 0.188 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.2145
7140
5 %
RANDOM
Rwork
0.17875
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obs
0.18053
135680
97.89 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK