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4EG0

Crystal Structure of D-alanine--D-alanine ligase from Burkholderia ambifaria

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008360biological_processregulation of cell shape
A0008716molecular_functionD-alanine-D-alanine ligase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008360biological_processregulation of cell shape
B0008716molecular_functionD-alanine-D-alanine ligase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 401
ChainResidue
ATYR90
AGLY92
AHOH592

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 402
ChainResidue
AGLU75
AASN277
AALA279

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO B 401
ChainResidue
BSER286
BLEU287
BPRO288
BHOH588
BARG260
BPRO280
BGLY281

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO B 402
ChainResidue
BPRO235
BALA236

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 403
ChainResidue
BASP39

Functional Information from PROSITE/UniProt
site_idPS00843
Number of Residues12
DetailsDALA_DALA_LIGASE_1 D-alanine--D-alanine ligase signature 1. HGgyGENGqIQG
ChainResidueDetails
AHIS70-GLY81

site_idPS00844
Number of Residues29
DetailsDALA_DALA_LIGASE_2 D-alanine--D-alanine ligase signature 2. LgctDwGRADFMldaagnay....FlEVNTaPG
ChainResidueDetails
ALEU253-GLY281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00047
ChainResidueDetails
AVAL138
AASP262
AGLU275
AASN277
BVAL138
BASP262
BGLU275
BASN277

220113

PDB entries from 2024-05-22

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