Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2D1F

Structure of Mycobacterium tuberculosis threonine synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004795molecular_functionthreonine synthase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006520biological_processamino acid metabolic process
A0008652biological_processamino acid biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0016829molecular_functionlyase activity
A0019344biological_processcysteine biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A1901605biological_processalpha-amino acid metabolic process
B0004795molecular_functionthreonine synthase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006520biological_processamino acid metabolic process
B0008652biological_processamino acid biosynthetic process
B0009088biological_processthreonine biosynthetic process
B0016829molecular_functionlyase activity
B0019344biological_processcysteine biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B1901605biological_processalpha-amino acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 500
ChainResidue
ASER67
AASN200
AGLU296
ATHR326
AHOH503
AHOH507
AHOH524
APHE68
ALYS69
AASN95
AVAL195
AGLY196
AASN197
AALA198
AGLY199

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP B 500
ChainResidue
BSER67
BPHE68
BLYS69
BASN95
BVAL195
BGLY196
BASN197
BALA198
BGLY199
BASN200
BGLU296
BALA298
BTHR326
BGLY327
BHOH502
BHOH503
BHOH507

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Eglnp.TGSFKDRGM
ChainResidueDetails
AGLU60-MET73

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18621388","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"18621388","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsCross-link: {"description":"Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)","evidences":[{"source":"PubMed","id":"20066036","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pwh
ChainResidueDetails
ALYS69

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pwh
ChainResidueDetails
BLYS69

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon