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3WLX

Crystal structure of low-specificity L-threonine aldolase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0006545biological_processglycine biosynthetic process
A0006567biological_processthreonine catabolic process
A0008732molecular_functionL-allo-threonine aldolase activity
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0050179molecular_functionphenylserine aldolase activity
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0006545biological_processglycine biosynthetic process
B0006567biological_processthreonine catabolic process
B0008732molecular_functionL-allo-threonine aldolase activity
B0016829molecular_functionlyase activity
B0030170molecular_functionpyridoxal phosphate binding
B0042802molecular_functionidentical protein binding
B0050179molecular_functionphenylserine aldolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLG B 401
ChainResidue
AARG229
BALA168
BARG169
BLYS197
BARG308
BHOH540
BHOH543
BHOH548
BHOH598
BSER6
BTHR8
BTHR57
BGLY58
BTHR59
BHIS83
BGLU136
BASP166

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLG A 401
ChainResidue
ASER6
ATHR57
AGLY58
ATHR59
AHIS83
AASP166
AALA168
AARG169
ALYS197
AARG308
AHOH512
AHOH525
AHOH531
AHOH571
BARG229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
BLYS197
ALYS197

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PDB entries from 2024-10-09

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