Structure of PDB 4p68 Chain A

Receptor sequence
>4p68A (length=159) Species: 562 (Escherichia coli) [Search protein sequence]
MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESI
GRPCPGRKNIILSSQPGTDDRVTWVKSVDEAIAAAGDVPEIMVIGGGRVY
EQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHS
YSFEILERR
3D structure
PDB4p68 Probing the electrostatics of active site microenvironments along the catalytic cycle for Escherichia coli dihydrofolate reductase.
ChainA
Resolution2.26 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 M20 W22 D27 L28 F31 C54 I91 T113
Catalytic site (residue number reindexed from 1) I5 M20 W22 D27 L28 F31 C54 I91 T113
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 MTX A I5 A6 M20 D27 F31 I50 X54 R57 I94 I5 A6 M20 D27 F31 I50 X54 R57 I94
BS02 NAP A A7 I14 N18 A19 M20 G43 R44 H45 T46 L62 S63 S64 I94 G96 G97 R98 V99 Q102 A7 I14 N18 A19 M20 G43 R44 H45 T46 L62 S63 S64 I94 G96 G97 R98 V99 Q102
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
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:4p68, PDBe:4p68, PDBj:4p68
PDBsum4p68
PubMed24977791
UniProtC3TR70

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