Structure of PDB 4b4w Chain A

Receptor sequence

>4b4wA (length=282) Species: 575584 (Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841)

MALVLDGRALAKQIEENLLVRVEALKAKTGRTPILATILVGDDGASATYV
RMKGNACRRVGMDSLKIELPQETTTEQLLAEIEKLNANPDVHGILLQHPV
PAQIDERACFDAISLAKDVDGVTCLGFGRMAMGEAAYGSATPAGIMTILK
ENNIEIAGKHAVVVGRSAILGKPMAMMLLQANATVTICHSRTQNLPELVK
QADIIVGAVGKAELIQKDWIKQGAVVVDAGFHPRDGGGVGDIQLQGIEEI
ASAYTPVPGGVGPMTITTLIRQTVEAAEKALG

3D structure

• PDB: 4b4w Acinetobacter Baumannii Fold Ligand Complexes; Potent Inhibitors of Folate Metabolism and a Re-Evaluation of the Ly374571 Structure.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S46 K53 Q97 D120
• Catalytic site (residue number reindexed from 1): S46 K53 Q97 D120
• Enzyme Commision number: 1.5.1.5: methylenetetrahydrofolate dehydrogenase (NADP(+)).
  3.5.4.9: methenyltetrahydrofolate cyclohydrolase.

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	NAP	A	R166 H189 S190 L195 V209 K211 L214	R166 H189 S190 L195 V209 K211 L214
BS02	9L9	A	Y49 K53 Q97 H98 D120 F231 P258 G259 G262	Y49 K53 Q97 H98 D120 F231 P258 G259 G262

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0003824 catalytic activity
• GO:0004477 methenyltetrahydrofolate cyclohydrolase activity
• GO:0004488 methylenetetrahydrofolate dehydrogenase (NADP+) activity
• GO:0016491 oxidoreductase activity
• GO:0016787 hydrolase activity

Biological Process

• GO:0000105 L-histidine biosynthetic process
• GO:0006164 purine nucleotide biosynthetic process
• GO:0006730 one-carbon metabolic process
• GO:0009086 methionine biosynthetic process
• GO:0035999 tetrahydrofolate interconversion

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:4b4w, PDBe:4b4w, PDBj:4b4w
• PDBsum: 4b4w
• PubMed: 23050773
• UniProt: D0CBC8