Structure of PDB 5fr9 Chain K

Receptor sequence
>5fr9K (length=319) Species: 1667 (Arthrobacter sp.) [Search protein sequence]
YTHDTGLDYITYSDYELDPANPLAGGAAWIEGAFVPPSEARISIFDQGFY
TSDATYTTFHVWNGNAFRLGDHIERLFSNAESIRLIPPLTQDEVKEIALE
LVAKTELREAMVTVTITRGYSSTPFERDITKHRPQVYMSACPYQWIVPFD
RIRDGVHLMVAQSVRRTPRSSIDPQVKNFQWGDLIRAIQETHDRGFELPL
LLDCDNLLAEGPGFNVVVIKDGVVRSPGRAALPGITRKTVLEIAESLGHE
AILADITPAELYDADEVLGCSTGGGVWPFVSVDGNSISDGVPGPVTQSII
RRYWELNVEPSSLLTPVQY
3D structure
PDB5fr9 Catalytic Promiscuity of Transaminases: Preparation of Enantioenriched Beta-Fluoroamines by Formal Tandem Hydrodefluorination/Deamination.
ChainK
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) Y56 K177 E210 L232
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 K R86 K188 E221 G224 F225 L243 G245 I246 T247 S282 T283 R75 K177 E210 G213 F214 L232 G234 I235 T236 S271 T272
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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