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1UAG

UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE

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
A0016881molecular_functionacid-amino acid ligase activity
A0042802molecular_functionidentical protein binding
A0051301biological_processcell division
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 964
ChainResidue
AASN113
AGLY114
ALYS115
ASER116
ATHR117
AARG302
ALYS319
AHOH643
AHOH646

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 965
ChainResidue
AASN7
AARG32
AGLU308
AHIS309
AASN310
AHOH524
AHOH637

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE UMA A 963
ChainResidue
ALEU15
ATHR16
AASP35
ATHR36
AARG37
ASER71
APRO72
AGLY73
AGLY137
AASN138
AGLY140
APHE161
AGLN162
AHIS183
AHOH501
AHOH502
AHOH529
AHOH554
AHOH565
AHOH594
AHOH600
AHOH682
AHOH684
AHOH712

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_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 10356330
ChainResidueDetails
AASN138
AHIS183
ALYS115

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 2026-03-25

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