Structure of PDB 3lg4 Chain B

Receptor sequence
>3lg4B (length=157) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
TLSILVAHDLQRVIGFENQLPWHLPNDLKHYKKLSTGHTLVMGRKTFESI
GKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIIGGQTLFEE
MIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHT
FLHLIRK
3D structure
PDB3lg4 Predicting resistance mutations using protein design algorithms.
ChainB
Resolution3.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L5 L20 W22 D27 L28 Y31 L54 V89 T111
Catalytic site (residue number reindexed from 1) L5 L20 W22 D27 L28 Y31 L54 V89 T111
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 V6 A7 I14 N18 Q19 L20 G43 R44 K45 T46 L62 T63 S64 I92 G93 G94 Q95 T96 E100 T121 V6 A7 I14 N18 Q19 L20 G43 R44 K45 T46 L62 T63 S64 I92 G93 G94 Q95 T96 E100 T121
BS02 52V B L5 V6 A7 Q19 L20 D27 L28 Y31 I50 I92 L5 V6 A7 Q19 L20 D27 L28 Y31 I50 I92
Gene Ontology
Molecular Function
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:0005829 cytosol

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Molecular Function

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Cellular Component
External links
PDB RCSB:3lg4, PDBe:3lg4, PDBj:3lg4
PDBsum3lg4
PubMed20643959
UniProtP0A017|DYR_STAAU Dihydrofolate reductase (Gene Name=folA)

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