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1EEH

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

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 UMA A 450
ChainResidue
AGLY14
AGLY137
AASN138
AGLY140
AGLN162
AHIS183
AHOH502
AHOH554
AHOH565
AHOH684
AHOH1130
ALEU15
AHOH1146
ATHR16
AASP35
ATHR36
AARG37
ASER71
APRO72
AGLY73

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
ASER112

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 317
ChainResidueDetails
ASER116activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
AILE139electrostatic stabiliser, hydrogen bond donor, steric role
AMET184hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role

218853

PDB entries from 2024-04-24

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