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

5A5F

CRYSTAL STRUCTURE OF MURD LIGASE FROM ESCHERICHIA COLI IN COMPLEX WITH UMA AND ADP

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 Residues24
DetailsBINDING SITE FOR RESIDUE UMA A 450
ChainResidue
AGLY14
AGLY137
AASN138
AGLY140
ASER159
AGLN162
AHIS183
AHOH2009
AHOH2010
AHOH2012
AHOH2059
ALEU15
AHOH2071
AHOH2095
AHOH2265
AHOH2266
AHOH2267
ATHR16
AASP35
ATHR36
AARG37
ASER71
APRO72
AGLY73

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ADP A 451
ChainResidue
AASN113
AGLY114
ALYS115
ASER116
ATHR117
AASN178
AHIS267
AASN271
AARG302
APHE303
AASP317
ALYS319
AALA320
ASER325
AALA328
AHOH2068
AHOH2071
AHOH2072
AHOH2074
AHOH2119
AHOH2184
AHOH2268

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MLI A 500
ChainResidue
ATHR321
AALA414
ASER415
AASN421
APHE422
AHOH2212

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MLI A 501
ChainResidue
AHIS241
ATHR246
AHIS334
AHOH2181
AHOH2269

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon