Structure of PDB 4m7u Chain A

Receptor sequence
>4m7uA (length=170) Species: 226185 (Enterococcus faecalis V583) [Search protein sequence]
MENLYFQGMLAAIWAQDEQGVIGKEGKLPWHLPNDLKFFKEKTIHNTLVL
GRATFEGMGCRPLPNRTTIVLTSNPDYQAEGVLVMHSVEEILAYADKYEG
VTVIGGGSVVFKELIPACDVLYRTMIHETFEGDTFFPEIDWSVWEKVATV
PGVVDEKNLYAHDYETYHRN
3D structure
PDB4m7u The Structure and Competitive Substrate Inhibition of Dihydrofolate Reductase from Enterococcus faecalis Reveal Restrictions to Cofactor Docking.
ChainA
Resolution2.1014 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I5 L20 W22 D27 L28 F31 L55 V93 T116
Catalytic site (residue number reindexed from 1) I13 L28 W30 D35 L36 F39 L63 V101 T124
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
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 W6 A7 I14 G15 G18 K19 L20 G43 R44 A45 T46 L63 T64 S65 H78 G97 G99 S100 V101 F103 E105 T126 W14 A15 I22 G23 G26 K27 L28 G51 R52 A53 T54 L71 T72 S73 H86 G105 G107 S108 V109 F111 E113 T134
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4m7u, PDBe:4m7u, PDBj:4m7u
PDBsum4m7u
PubMed24495113
UniProtQ834R2

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