Structure of PDB 3fmx Chain X

Receptor sequence

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

SFRIAAIPGDGIGLEVLPEGIRVLEAAALKHGLALEFDTFEWASCDYYLQ
HGKMMPDDWAEQLKQYDAIYFGAVGWPDKVPDHISLWGSLLKFRREFDQY
VNIRPVRLFPGVPCALANRKVGDIDFVVVRENTEGEYSSLGGIMFENTEN
EIVIQESIFTRRGVDRILKYAFDLAEKRERKHVTSATKSNGMAISMPYWD
KRTEAMAAHYPHVSWDKQHIDILCARFVLQPERFDVVVASNLFGDILSDL
GPACAGTIGIAPSANLNPERNFPSLFEPVHGSAPDIFGKNIANPIAMIWS
GALMLEFLGQGDERYQRAHDDMLNAIERVIADGSVTPDMGGTLSTQQVGA
AISDTLARL

3D structure

• PDB: 3fmx Structural Characterization of Tartrate Dehydrogenase: a versatile enzyme catalyzing multiple reactions
• Chain: X
• Resolution: 2.95 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Y141 K192 D225 D250
• Catalytic site (residue number reindexed from 1): Y137 K188 D221 D245
• 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	X	A77 V78 G79 D86 L94 I263 G264 E282 H285 G286 S287 A288 D290 N298 D343	A73 V74 G75 D82 L90 I258 G259 E277 H280 G281 S282 A283 D285 N293 D338

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:3fmx, PDBe:3fmx, PDBj:3fmx
• PDBsum: 3fmx
• UniProt: Q51945|TTUC_PSEPU Tartrate dehydrogenase/decarboxylase