Structure of PDB 3qlz Chain A

Receptor sequence
>3qlzA (length=225) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence]
KVPVVGIVAALLPEMGIGFQGNLPWRLAKEMKYFREVTTLTNDNSKQNVV
IMGRKTWESIPQKFRPLPKRINVVVSRSFDGELRKVEDGIYHSNSLRNCL
TALQSSLANENKIERIYIIGGGEIYRQSMDLADHWLITKIMPLPETTIPQ
MDTFLQKQELEQRFYDNSDKLVDFLPSSIQLEGRLTSQEWNGELVKGLPV
QEKGYQFYFTLYTKKLEHHHHHHHH
3D structure
PDB3qlz Crystal Structures of Candida albicans Dihydrofolate Reductase Bound to Propargyl-Linked Antifolates Reveal the Flexibility of Active Site Loop Residues Critical for Ligand Potency and Selectivity.
ChainA
Resolution1.94 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A V10 A11 I19 G23 N24 L25 G55 R56 K57 T58 V77 S78 R79 N96 S97 L98 I121 G123 G124 E125 I126 Q129 V8 A9 I17 G21 N22 L23 G53 R54 K55 T56 V75 S76 R77 N94 S95 L96 I119 G121 G122 E123 I124 Q127
BS02 QLZ A I9 V10 A11 L25 E32 M33 F36 I62 I121 I7 V8 A9 L23 E30 M31 F34 I60 I119 MOAD: ic50=15nM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3qlz, PDBe:3qlz, PDBj:3qlz
PDBsum3qlz
PubMed21726415
UniProtQ6FPH0

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