Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5A5E

CRYSTAL STRUCTURE OF MURD LIGASE FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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 Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 502
ChainResidue
ALEU15
AALA212
AMET218
ASER229
AHOH2020

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A 650
ChainResidue
AGLU253
AHIS309

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 800
ChainResidue
ASER160
ATYR194
ALYS198
AHOH2109
AHOH2124
AGLY111
ALYS115

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 801
ChainResidue
ATHR321
AALA414
ASER415
ALEU416
AASN421
APHE422
AHOH2297

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 802
ChainResidue
ASER264
AGLY265
ATYR269
AHIS334
AHOH2192

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 803
ChainResidue
AALA282
AGLY283
AARG400

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 804
ChainResidue
AGLY14
ALEU15
ATHR16
AHOH2010
AHOH2011
AHOH2059

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1441
ChainResidue
AGLY114
ALYS115
ASER116
ATHR117
AARG302
ALYS319
AHOH2096
AHOH2234

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 Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 317
ChainResidueDetails
ALYS115activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
AASN138electrostatic stabiliser, hydrogen bond donor, steric role

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon