Structure of PDB 2jff Chain A Binding Site BS01

Receptor Information
>2jff Chain A (length=433) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAV
ERHTGSLNDEWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCR
EAQAPIVAITGSNGKSTVTTLVGEMAKAAGVNVGVGGNIGLPALMLLDDE
CELYVLELSSFQLETTSSLQAVAATILNVTEDHMDRYPFGLQQYRAAKLR
IYENAKVCVVNADDALTMPIRRCVSFGVNMGDYHLNHQETWLRVKGEKVL
NVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGLPHRFEVV
LEHNGVRWINDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLA
RYLNGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDM
VLLSPACASLDQFKNFEQRGNEFARLAKELGSH
Ligand information
Ligand IDLK2
InChIInChI=1S/C19H23NO7S/c1-2-3-10-27-15-6-4-14-12-16(7-5-13(14)11-15)28(25,26)20-17(19(23)24)8-9-18(21)22/h4-7,11-12,17,20H,2-3,8-10H2,1H3,(H,21,22)(H,23,24)/t17-/m1/s1
InChIKeyUAGYXJBYAFGRFR-QGZVFWFLSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CCCCOc1ccc2cc(ccc2c1)[S](=O)(=O)N[CH](CCC(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0CCCCOc1ccc2cc(ccc2c1)S(=O)(=O)N[C@H](CCC(=O)O)C(=O)O
ACDLabs 10.04O=C(O)C(NS(=O)(=O)c1ccc2c(c1)ccc(OCCCC)c2)CCC(=O)O
OpenEye OEToolkits 1.5.0CCCCOc1ccc2cc(ccc2c1)S(=O)(=O)NC(CCC(=O)O)C(=O)O
CACTVS 3.341CCCCOc1ccc2cc(ccc2c1)[S](=O)(=O)N[C@H](CCC(O)=O)C(O)=O
FormulaC19 H23 N O7 S
NameN-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-D-GLUTAMIC ACID
ChEMBLCHEMBL528988
DrugBankDB08106
ZINCZINC000016052242
PDB chain2jff Chain A Residue 1440 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2jff Structural and Functional Characterization of Enantiomeric Glutamic Acid Derivatives as Potential Transition State Analogue Inhibitors of Murd Ligase.
Resolution1.89 Å
Binding residue
(original residue number in PDB)		R37 G73 F161 H183 K348 A414 S415 F422
Binding residue
(residue number reindexed from 1)		R37 G73 F161 H183 K342 A408 S409 F416
Annotation score1
Binding affinityMOAD: Ki=240uM
BindingDB: Kd=210000nM,IC50=2.80e+5nM
Enzymatic activity
Catalytic site (original residue number in PDB) K115 S116 N138 L147 H183
Catalytic site (residue number reindexed from 1) K115 S116 N138 L147 H183
Enzyme Commision number 6.3.2.9: UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008764 UDP-N-acetylmuramoylalanine-D-glutamate ligase activity
GO:0016874 ligase activity
GO:0016881 acid-amino acid ligase activity
GO:0042802 identical protein binding
Biological Process
GO:0008360 regulation of cell shape
GO:0009058 biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0051301 cell division
GO:0071555 cell wall organization
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2jff, PDBe:2jff, PDBj:2jff
PDBsum2jff
PubMed17507028
UniProtP14900|MURD_ECOLI UDP-N-acetylmuramoylalanine--D-glutamate ligase (Gene Name=murD)

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