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2XPC

Second-generation sulfonamide inhibitors of MurD: Activity optimisation with conformationally rigid analogues of D-glutamic acid

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 Residues22
DetailsBINDING SITE FOR RESIDUE 051 A 500
ChainResidue
AILE11
ATHR321
ALYS348
AALA414
ASER415
AASN421
APHE422
ADMS602
AHOH2243
AHOH2245
AHOH2477
AGLY12
AHOH2478
AHOH2479
AHOH2480
AASP35
ATHR36
AARG37
ASER71
AGLY73
APHE161
AHIS183

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS A 601
ChainResidue
ALEU163
ATHR166
ASER167
ASER168
ALEU169
AARG200
AGLU203
AHOH2264

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS A 602
ChainResidue
AGLY73
AASP185
AARG186
A051500
AHOH2481

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE DMS A 604
ChainResidue
AASN7
AARG32
AALA64
AGLU308
AHIS309
AASN310
AHOH2098
AHOH2482

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1441
ChainResidue
AASN113
AGLY114
ALYS115
ASER116
ATHR117
AARG302
ALYS319
AHOH2483
AHOH2484

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1442
ChainResidue
AHIS309
AASN310
ASER438
AHIS439

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1444
ChainResidue
AGLY14
ALEU15
ATHR16
AHOH2485

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1445
ChainResidue
AARG37
AMET38
AGLN170
AHOH2487

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

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PDB entries from 2024-07-17

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