Structure of PDB 3ngl Chain A

Receptor sequence

>3nglA (length=275) Species: 2303 (Thermoplasma acidophilum)

KILRGEEIAEKKAENLHGIIERSGLEPSLKLIQIGDNEAASIYARAKIRR
GKKIGIAVDLEKYDDISMKDLLKRIDDLAKDPQINGIMIENPLPKGFDYY
EIVRNIPYYKDVDALSPYNQGLIALNREFLVPATPRAVIDIMDYYGYHEN
TVTIVNRSPVVGRPLSMMLLNRNYTVSVCHSKTKDIGSMTRSSKIVVVAV
GRPGFLNREMVTPGSVVIDVGINYVNDKVVGDANFEDLSEYVEAITPVPG
GVGPITATNILENVVKAAEFQKNNL

3D structure

• PDB: 3ngl Crystal structure of bifunctional 5,10-methylenetetrahydrofolate dehydrogenase/cyclohydrolase from Thermoplasma acidophilum
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): A41 K48 E91 D114
• Catalytic site (residue number reindexed from 1): A40 K47 E90 D113
• 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	T135 N157 R158 S159 H181 S182 A200 V201 F206 V221 I223	T134 N156 R157 S158 H180 S181 A199 V200 F205 V220 I222

Gene Ontology

Molecular Function

• 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:3ngl, PDBe:3ngl, PDBj:3ngl
• PDBsum: 3ngl
• PubMed: 21333632
• UniProt: Q05213|FOLD_THEAC Bifunctional protein FolD (Gene Name=folD)