Structure of PDB 3flk Chain A

Receptor sequence

>3flkA (length=359) Species: 303 (Pseudomonas putida)

SFRIAAIPGDGIGLEVLPEGIRVLEAAALKHGLALEFDTFEWASCDYYLQ
HGKMMPDDWAEQLKQYDAIYFGAVGWPDKVPDHISLWGSLLKFRREFDQY
VNIRPVRLFPGVPCALANRKVGDIDFVVVRENTEGEYSSLGGIMFENTEN
EIVIQESIFTRRGVDRILKYAFDLAEKRERKHVTSATKSNGMAISMPYWD
KRTEAMAAHYPHVSWDKQHIDILCARFVLQPERFDVVVASNLFGDILSDL
GPACAGTIGIAPSANLNPERNFPSLFEPVHGSAPDIFGKNIANPIAMIWS
GALMLEFLGQGDERYQRAHDDMLNAIERVIADGSVTPDMGGTLSTQQVGA
AISDTLARL

3D structure

• PDB: 3flk Structural characterization of tartrate dehydrogenase: a versatile enzyme catalyzing multiple reactions.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y141 K192 D225 D250 D254
• Catalytic site (residue number reindexed from 1): Y137 K188 D221 D245 D249
• Enzyme Commision number: 1.1.1.83: D-malate dehydrogenase (decarboxylating).
  1.1.1.93: tartrate dehydrogenase.
  4.1.1.73: tartrate decarboxylase.

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	NAI	A	I16 A77 V78 G79 D86 L94 I263 H285 G286 S287 A288 I291 N298	I12 A73 V74 G75 D82 L90 I258 H280 G281 S282 A283 I286 N293
BS02	OXL	A	R98 R108 R134 D250	R94 R104 R130 D245
BS03	NAI	A	N194 I226 R230	N190 I222 R226

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0009027 tartrate dehydrogenase activity
• GO:0016491 oxidoreductase activity
• GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
• GO:0016829 lyase activity
• GO:0046553 D-malate dehydrogenase (decarboxylating) (NAD+) activity
• GO:0046872 metal ion binding
• GO:0050319 tartrate decarboxylase activity
• GO:0051287 NAD binding

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3flk, PDBe:3flk, PDBj:3flk
• PDBsum: 3flk
• PubMed: 20516620
• UniProt: Q51945|TTUC_PSEPU Tartrate dehydrogenase/decarboxylase