Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2Y66

New 5-Benzylidenethiazolidine-4-one Inhibitors of Bacterial MurD Ligase: Design, Synthesis, Crystal Structures, and Biological Evaluation

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008360biological_processregulation of cell shape
A0008764molecular_functionUDP-N-acetylmuramoylalanine-D-glutamate ligase activity
A0009058biological_processbiosynthetic process
A0009252biological_processpeptidoglycan biosynthetic process
A0016874molecular_functionligase activity
A0016881molecular_functionacid-amino acid ligase activity
A0042802molecular_functionidentical protein binding
A0051301biological_processcell division
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE N04 A 500
ChainResidue
AILE11
AALA414
ASER415
AASN421
APHE422
ASO31441
AHOH2021
AHOH2349
AHOH2457
AASP35
ATHR36
AARG37
ASER71
APRO72
APHE161
AHIS183
ALYS348

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS A 601
ChainResidue
ALEU163
ATHR166
ASER167
ASER168
ALEU169
AARG200
AGLU203
AHOH2245

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1440
ChainResidue
AASN113
AGLY114
ALYS115
ASER116
ATHR117
AARG302
ALYS319
AHOH2458

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO3 A 1441
ChainResidue
AGLY14
ALEU15
ATHR16
AN04500
AHOH2459

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1442
ChainResidue
ALEU57
AHOH2110
AHOH2113

Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. GSNGKSTVTTLVGEMA
ChainResidueDetails
AGLY111-ALA126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY111

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 317
ChainResidueDetails
ALYS115activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
AASN138electrostatic stabiliser, hydrogen bond donor, steric role
AHIS183hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon