Structure of PDB 3pyz Chain A

Receptor sequence

>3pyzA (length=410) Species: 214092 (Yersinia pestis CO92)

QTPQATSPLAAWLCYLEHLHSQPIELGLERVKQVAERLDLLKPAPKIFTV
AGTNGKGTTCCTLEAILLAAGLRVGVYSSPHLLRYTERVRIQGQELSEAE
HSHSFAQIEAGRGDISLTYFEFGTLSALQLFKQAKLDVVILEVGLGGRLD
ATNIVDSDVAAITSIALDHTDWLGYDRESIGREKAGVFRGGKPAVVGEPD
MPQSIADVAAELGAQLYRRDVAWKFSQQNGWHWQCGERQLTGLPVPNVPL
ANAATALAVLHYSELPLSDEAIRQGLQAASLPGRFQVVSEQPLLILDVAH
NPHAARYLVNRLAQVIQGKVRAVVGMLSDKDIAGTLACLSERVDEWYCAP
LEGPRGASAGQLAEHLVSARQFSDVETAWRQAMQDADTQDVVIVCGSFHT
VAHVMAALHL

3D structure

• PDB: 3pyz Crystal structure of bifunctional folylpolyglutamate synthase/dihydrofolate synthase complexed with AMPpnp and Mn ion from Yersinia pestis c092
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Enzyme Commision number: 6.3.2.12: dihydrofolate synthase.
  6.3.2.17: tetrahydrofolate synthase.

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	ANP	A	N58 G59 K60 G61 T62 N269 R301 D314 V315 H320 A321 Y324 F422	N54 G55 K56 G57 T58 N252 R284 D297 V298 H303 A304 Y307 F398
BS02	MN	A	S83 E146	S79 E142

Gene Ontology

Molecular Function

• GO:0004326 tetrahydrofolylpolyglutamate synthase activity
• GO:0005524 ATP binding
• GO:0008841 dihydrofolate synthase activity
• GO:0016874 ligase activity
• GO:0016881 acid-amino acid ligase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006761 dihydrofolate biosynthetic process
• GO:0009058 biosynthetic process
• GO:0009396 folic acid-containing compound biosynthetic process
• GO:0046654 tetrahydrofolate biosynthetic process
• GO:0046656 folic acid biosynthetic process
• GO:0046901 tetrahydrofolylpolyglutamate biosynthetic process

External links

• PDB: RCSB:3pyz, PDBe:3pyz, PDBj:3pyz
• PDBsum: 3pyz
• UniProt: Q8D0U0