Structure of PDB 3eek Chain B

Receptor sequence

>3eekB (length=225) Species: 5478 (Nakaseomyces glabratus)

KVPVVGIVAALLPEMGIGFQGNLPWRLAKEMKYFREVTTLTNDNSKQNVV
IMGRKTWESIPQKFRPLPKRINVVVSRSFDGELRKVEDGIYHSNSLRNCL
TALQSSLANENKIERIYIIGGGEIYRQSMDLADHWLITKIMPLPETTIPQ
MDTFLQKQELEQRFYDNSDKLVDFLPSSIQLEGRLTSQEWNGELVKGLPV
QEKGYQFYFTLYTKKLEHHHHHHHH

3D structure

• PDB: 3eek Probing the active site of Candida glabrata dihydrofolate reductase with high resolution crystal structures and the synthesis of new inhibitors
• Chain: B
• Resolution: 2.03 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L25 W27 E32 M33 F36 L69 I118 T140
• Catalytic site (residue number reindexed from 1): L23 W25 E30 M31 F34 L67 I116 T138
• 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	NDP	B	V10 A11 I19 G23 N24 L25 G55 R56 K57 T58 V77 S78 R79 N96 S97 I121 G123 G124 E125 I126 Q129	V8 A9 I17 G21 N22 L23 G53 R54 K55 T56 V75 S76 R77 N94 S95 I119 G121 G122 E123 I124 Q127
BS02	53S	B	I9 V10 L25 E32 M33 F36 S61 I62 P63 F66 I121	I7 V8 L23 E30 M31 F34 S59 I60 P61 F64 I119	MOAD: ic50=0.61nM BindingDB: IC50=0.61nM

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:0005575 cellular_component
• GO:0005739 mitochondrion

External links

• PDB: RCSB:3eek, PDBe:3eek, PDBj:3eek
• PDBsum: 3eek
• PubMed: 19152636
• UniProt: Q6FPH0