Structure of PDB 5ecx Chain A

Receptor sequence
>5ecxA (length=157) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
MKLSLMVAISKNGVIGNGPDIPWSAKGEQLLFKAITYNQWLLVGRKTFES
MGALPNRKYAVVTRSSFTSDNENVLIFPSIKDALTNLKKITDHVIVSGGG
EIYKSLIDQVDTLHISTIDIEPEGDVYFPEIPSNFRPVFTQDFASNINYS
YQIWQKG
3D structure
PDB5ecx Crystal Structures of Trimethoprim-Resistant DfrA1 Rationalize Potent Inhibition by Propargyl-Linked Antifolates.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M5 I20 W22 E27 Q28 F31 L53 V93 S115
Catalytic site (residue number reindexed from 1) M6 I21 W23 E28 Q29 F32 L54 V94 S116
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 V6 A7 I14 G17 P18 D19 I20 G43 R44 K45 T46 V61 T62 R63 P77 S78 I79 G98 G99 E100 I101 V7 A8 I15 G18 P19 D20 I21 G44 R45 K46 T47 V62 T63 R64 P78 S79 I80 G99 G100 E101 I102
BS02 5N1 A M5 V6 A7 E27 Q28 F31 M50 L53 M6 V7 A8 E28 Q29 F32 M51 L54
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5ecx, PDBe:5ecx, PDBj:5ecx
PDBsum5ecx
PubMed27624966
UniProtA4GRC7

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