Structure of PDB 6ecp Chain A

Receptor sequence
>6ecpA (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
APAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNL
YINVKLKAAEEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQL
PLDSENSINTEEVINAIAPEKDVDGLTSINAGRLARGDLNDCFIPCTPKG
CLELIKETGVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAH
LDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPKVVGDVAYD
EAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLE
3D structure
PDB6ecp An assessment of three human methylenetetrahydrofolate dehydrogenase/cyclohydrolase-ligand complexes following further refinement.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S49 K56 Q100 D125
Catalytic site (residue number reindexed from 1) S48 K55 Q99 D124
Enzyme Commision number 1.5.1.5: methylenetetrahydrofolate dehydrogenase (NADP(+)).
3.5.4.9: methenyltetrahydrofolate cyclohydrolase.
6.3.4.3: formate--tetrahydrofolate 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 NAP A T148 R173 S174 V177 H196 S197 A215 T216 G217 C236 I238 T279 T147 R172 S173 V176 H195 S196 A214 T215 G216 C235 I237 T270
BS02 21V A Y52 K56 P272 G273 G276 P277 V280 Y51 K55 P263 G264 G267 P268 V271
BS03 21V A Y52 V55 P272 G276 V280 Y51 V54 P263 G267 V271
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004488 methylenetetrahydrofolate dehydrogenase (NADP+) activity

View graph for
Molecular Function
External links
PDB RCSB:6ecp, PDBe:6ecp, PDBj:6ecp
PDBsum6ecp
PubMed30839287
UniProtP11586|C1TC_HUMAN C-1-tetrahydrofolate synthase, cytoplasmic (Gene Name=MTHFD1)

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