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CRYSTAL STRUCTURE OF MURD LIGASE IN COMPLEX WITH D-GLU CONTAINING RHODANINE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0007049biological_processcell cycle
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 Residues20
DetailsBINDING SITE FOR RESIDUE D17 A 1441
ChainResidue
AILE11
AALA414
ASER415
ALEU416
AASN421
APHE422
ASO41451
AHOH2525
AHOH2526
AHOH2528
AHOH2529
AASP35
AHOH2530
ATHR36
AARG37
ASER71
APRO72
APHE161
AHIS183
ALYS348

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DMS A 1442
ChainResidue
AGLY73
AARG186
ALEU416
AHOH2265
AHOH2529
AHOH2531

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE AZI A 1443
ChainResidue
AASP417
AGLN418
APHE419

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AZI A 1444
ChainResidue
AALA329
AASN331
ALEU333
AHOH2532

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AZI A 1445
ChainResidue
APRO300
AARG302
APHE422
AGLU423

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE AZI A 1446
ChainResidue
ALEU339
AASN363

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE AZI A 1447
ChainResidue
AALA102
AALA104
APRO105
AHOH2164

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1448
ChainResidue
AASN113
AGLY114
ALYS115
ASER116
ATHR117
AARG302
AHOH2533
AHOH2534

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1449
ChainResidue
ATHR166
ASER167
ASER168
ALEU169
AARG200
AGLU203

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1450
ChainResidue
AHIS309
AASN310
ASER438
AHIS439

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1451
ChainResidue
AGLY14
ALEU15
ATHR16
AD171441
AHOH2024
AHOH2526
AHOH2535
AHOH2536

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1452
ChainResidue
AARG37
AMET38
AGLN170
AHOH2537

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1453
ChainResidue
AHIS309
AASN310
AHOH2055
AHOH2057

site_idBC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 1454
ChainResidue
AARG395

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1455
ChainResidue
ATYR3
AGLN4
AARG27

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 1456
ChainResidue
AGLU96
ATHR165
ASER167
AHOH2149

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1457
ChainResidue
ALEU57
AHOH2127

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

218853

PDB entries from 2024-04-24

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