Structure of PDB 4elb Chain D

Receptor sequence
>4elbD (length=166) Species: 260799 (Bacillus anthracis str. Sterne) [Search protein sequence]
MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEA
IGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCKNEEEIFIFGGAQ
IYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNP
YTYYYHVYEKQQLVPR
3D structure
PDB4elb Structure-activity relationship for enantiomers of potent inhibitors of B. anthracis dihydrofolate reductase.
ChainD
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M6 L21 W23 E28 L29 V32 L55 I93 T115
Catalytic site (residue number reindexed from 1) M6 L21 W23 E28 L29 V32 L55 I93 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 CA D Y108 D110 Y108 D110
BS02 34R D M6 V7 A8 L21 E28 L29 V32 I51 R53 L55 F96 M6 V7 A8 L21 E28 L29 V32 I51 R53 L55 F96
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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External links
PDB RCSB:4elb, PDBe:4elb, PDBj:4elb
PDBsum4elb
PubMed22999981
UniProtQ81R22

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