Structure of PDB 1u3g Chain A

Receptor sequence
>1u3gA (length=164) Species: 2104 (Mycoplasmoides pneumoniae) [Search protein sequence]
MDKNALRKQILQKRMALSTIEKSHLDQKINQKLVAFLTPKPCIKTIALYE
PIKNEVTFVDFFFEFLKINQIRAVYPKVISDTEIIFIDQETNTFEPNQID
CFLIPLVGFNKDNYRLGFGKGYYDRYLMQLTRQQPKIGIAYSFQKGDFLA
DPWDVQLDLIINDE
3D structure
PDB1u3g Crystal structure of methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae (GI: 13508087) at 2.2 A resolution
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R115 D124 D154
Catalytic site (residue number reindexed from 1) R115 D124 D154
Enzyme Commision number 6.3.3.2: 5-formyltetrahydrofolate cyclo-ligase.
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 MG A D124 D154 D124 D154
BS02 ADP A R7 G117 G119 K120 G121 D124 R125 M128 W153 R7 G117 G119 K120 G121 D124 R125 M128 W153
BS03 THF A E50 E55 P76 P105 R115 F118 K120 Y122 Y123 E50 E55 P76 P105 R115 F118 K120 Y122 Y123
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0030272 5-formyltetrahydrofolate cyclo-ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0035999 tetrahydrofolate interconversion
Cellular Component
GO:0005737 cytoplasm

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Cellular Component
External links
PDB RCSB:1u3g, PDBe:1u3g, PDBj:1u3g
PDBsum1u3g
PubMed15281135
UniProtP75430|MTHFS_MYCPN 5-formyltetrahydrofolate cyclo-ligase (Gene Name=MPN_348)

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