Structure of PDB 2jfh Chain A Binding Site BS01

Receptor Information
>2jfh Chain A (length=430) 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
IYENAKVCVVNADDALTMPIRCVSFGVNMGDYHLNETWLRVKGEKVLNVK
EMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGLPHRFEVVLEH
NGVRWINDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLARYL
NGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDMVLL
SPACASLDQFKNFEQRGNEFARLAKELGSH
Ligand information
Ligand IDLK1
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-/m0/s1
InChIKeyUAGYXJBYAFGRFR-KRWDZBQOSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CCCCOc1ccc2cc(ccc2c1)[S](=O)(=O)N[C@@H](CCC(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0CCCCOc1ccc2cc(ccc2c1)S(=O)(=O)N[C@@H](CCC(=O)O)C(=O)O
CACTVS 3.341CCCCOc1ccc2cc(ccc2c1)[S](=O)(=O)N[CH](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
FormulaC19 H23 N O7 S
NameN-[(6-BUTOXYNAPHTHALEN-2-YL)SULFONYL]-L-GLUTAMIC ACID
ChEMBLCHEMBL458624
DrugBankDB08105
ZINCZINC000016052243
PDB chain2jfh Chain A Residue 1441 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2jfh Structural and Functional Characterization of Enantiomeric Glutamic Acid Derivatives as Potential Transition State Analogue Inhibitors of Murd Ligase.
Resolution1.97 Å
Binding residue
(original residue number in PDB)		T36 R37 G73 H183 K348 A414 S415 L416 N421 F422 H439
Binding residue
(residue number reindexed from 1)		T36 R37 G73 H183 K339 A405 S406 L407 N412 F413 H430
Annotation score1
Binding affinityMOAD: Ki=870uM
PDBbind-CN: -logKd/Ki=3.06,Ki=870uM
BindingDB: IC50=7.10e+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:2jfh, PDBe:2jfh, PDBj:2jfh
PDBsum2jfh
PubMed17507028
UniProtP14900|MURD_ECOLI UDP-N-acetylmuramoylalanine--D-glutamate ligase (Gene Name=murD)

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