Structure of PDB 5hi6 Chain A

Receptor sequence
>5hi6A (length=161) Species: 214092 (Yersinia pestis CO92) [Search protein sequence]
AMIISLIAALAADRVIGMENAMPWHLPADLAWFKRNTLNKPVIMGRKTFE
SIGRPLPGRLNIVISSQPGTDERVTWAASIEEALAFAGNAEEVMVMGGGR
VYKQFLDRANRMYLTHIDAEVGGDTHFPDYEPDEWESVFSEFHDADEANS
HSYCFEILERR
3D structure
PDB5hi6 The high resolution structure of dihydrofolate reductase from Yersinia pestis complex with methotrexate as closed form
ChainA
Resolution2.051 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I6 M21 W23 D28 L29 F32 L55 V92 T114
Catalytic site (residue number reindexed from 1) I7 M22 W24 D29 L30 F33 L56 V93 T115
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 I6 A7 D28 F32 K33 I51 R58 M95 I7 A8 D29 F33 K34 I52 R59 M96
BS02 CA A M17 E18 M18 E19
Gene Ontology
Molecular Function
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5hi6, PDBe:5hi6, PDBj:5hi6
PDBsum5hi6
PubMed
UniProtA0A3N4BLI0

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