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1VB3

Crystal Structure of Threonine Synthase from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0004795molecular_functionthreonine synthase activity
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0009088biological_processthreonine biosynthetic process
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
ASER247
AGLY248
AASN249
APHE250
AGLY251
AASP252
AKPA500
AHOH538
AHOH672

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE KPA A 500
ChainResidue
ALYS107
ATHR133
ASER134
AASP136
ATHR137
APHE186
AASN212
ASER213
AARG218
AASN249
ASO4501
AHOH503
AHOH538
AHOH630

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues15
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. ElfhgpTLAFKDFGG
ChainResidueDetails
AGLU97-GLY111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS107

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pwh
ChainResidueDetails
ALYS107

223166

PDB entries from 2024-07-31

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