Structure of PDB 3srr Chain X

Receptor sequence
>3srrX (length=157) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
TLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESI
GKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEE
MIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHT
FLHLIRK
3D structure
PDB3srr Structure-based design of new DHFR-based antibacterial agents: 7-aryl-2,4-diaminoquinazolines.
ChainX
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L6
Catalytic site (residue number reindexed from 1) L5
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 Q20 X L6 V7 A8 L21 D28 L29 V32 I51 F93 L5 V6 A7 L20 D27 L28 V31 I50 F92 MOAD: Ki=0.24nM
BindingDB: Ki=0.24nM
BS02 NAP X V7 A8 I15 G16 N19 Q20 L21 G44 R45 K46 T47 L63 T64 S65 F93 G95 Q96 T97 E101 T122 V6 A7 I14 G15 N18 Q19 L20 G43 R44 K45 T46 L62 T63 S64 F92 G94 Q95 T96 E100 T121
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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Biological Process
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Cellular Component
External links
PDB RCSB:3srr, PDBe:3srr, PDBj:3srr
PDBsum3srr
PubMed21831637
UniProtP0A017|DYR_STAAU Dihydrofolate reductase (Gene Name=folA)

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