Structure of PDB 5fr9 Chain G

Receptor sequence
>5fr9G (length=321) Species: 1667 (Arthrobacter sp.) [Search protein sequence]
IVYTHDTGLDYITYSDYELDPANPLAGGAAWIEGAFVPPSEARISIFDQG
FYTSDATYTTFHVWNGNAFRLGDHIERLFSNAESIRLIPPLTQDEVKEIA
LELVAKTELREAMVTVTITRGYSSTPFERDITKHRPQVYMSACPYQWIVP
FDRIRDGVHLMVAQSVRRTPRSSIDPQVKNFQWGDLIRAIQETHDRGFEL
PLLLDCDNLLAEGPGFNVVVIKDGVVRSPGRAALPGITRKTVLEIAESLG
HEAILADITPAELYDADEVLGCSTGGGVWPFVSVDGNSISDGVPGPVTQS
IIRRYWELNVEPSSLLTPVQY
3D structure
PDB5fr9 Catalytic Promiscuity of Transaminases: Preparation of Enantioenriched Beta-Fluoroamines by Formal Tandem Hydrodefluorination/Deamination.
ChainG
Resolution2.81 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y67 K188 E221 L243
Catalytic site (residue number reindexed from 1) Y58 K179 E212 L234
Enzyme Commision number 2.6.1.18: beta-alanine--pyruvate transaminase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 9HC G R86 K188 E221 G224 F225 L243 G245 I246 T247 T283 R77 K179 E212 G215 F216 L234 G236 I237 T238 T274
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
Biological Process
GO:0019752 carboxylic acid metabolic process
GO:0046394 carboxylic acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5fr9, PDBe:5fr9, PDBj:5fr9
PDBsum5fr9
PubMed26836037
UniProtF7J696

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