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6NMX

Threonine synthase from Bacillus subtilis ATCC 6633 with PLP and APPA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003941molecular_functionL-serine ammonia-lyase activity
A0004794molecular_functionthreonine deaminase activity
A0004795molecular_functionthreonine synthase activity
A0006520biological_processamino acid metabolic process
A0006565biological_processL-serine catabolic process
A0006567biological_processthreonine catabolic process
A0009088biological_processthreonine biosynthetic process
A0009097biological_processisoleucine biosynthetic process
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
B0003941molecular_functionL-serine ammonia-lyase activity
B0004794molecular_functionthreonine deaminase activity
B0004795molecular_functionthreonine synthase activity
B0006520biological_processamino acid metabolic process
B0006565biological_processL-serine catabolic process
B0006567biological_processthreonine catabolic process
B0009088biological_processthreonine biosynthetic process
B0009097biological_processisoleucine biosynthetic process
B0016829molecular_functionlyase activity
B0030170molecular_functionpyridoxal phosphate binding
C0003941molecular_functionL-serine ammonia-lyase activity
C0004794molecular_functionthreonine deaminase activity
C0004795molecular_functionthreonine synthase activity
C0006520biological_processamino acid metabolic process
C0006565biological_processL-serine catabolic process
C0006567biological_processthreonine catabolic process
C0009088biological_processthreonine biosynthetic process
C0009097biological_processisoleucine biosynthetic process
C0016829molecular_functionlyase activity
C0030170molecular_functionpyridoxal phosphate binding
D0003941molecular_functionL-serine ammonia-lyase activity
D0004794molecular_functionthreonine deaminase activity
D0004795molecular_functionthreonine synthase activity
D0006520biological_processamino acid metabolic process
D0006565biological_processL-serine catabolic process
D0006567biological_processthreonine catabolic process
D0009088biological_processthreonine biosynthetic process
D0009097biological_processisoleucine biosynthetic process
D0016829molecular_functionlyase activity
D0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues26
Detailsbinding site for residue LJS A 401
ChainResidue
APHE58
AARG158
AVAL184
AGLY185
AASN186
AALA187
AGLY188
AASN189
AALA237
AILE238
AGLU284
ALYS59
ASER287
ATHR314
AHOH524
AHOH536
AHOH560
AHOH572
AHOH605
ASER82
ATHR83
AASN85
ATHR86
APHE132
AASN152
ASER153

site_idAC2
Number of Residues26
Detailsbinding site for residue LJS B 401
ChainResidue
BPHE58
BLYS59
BSER82
BTHR83
BASN85
BTHR86
BPHE132
BASN152
BSER153
BARG158
BVAL184
BGLY185
BASN186
BALA187
BGLY188
BASN189
BALA237
BILE238
BILE240
BGLU284
BTHR314
BHOH525
BHOH539
BHOH556
BHOH562
BHOH614

site_idAC3
Number of Residues26
Detailsbinding site for residue LJS C 401
ChainResidue
CPHE58
CLYS59
CSER82
CTHR83
CASN85
CTHR86
CPHE132
CASN152
CSER153
CARG158
CVAL184
CGLY185
CASN186
CALA187
CGLY188
CASN189
CALA237
CILE238
CILE240
CGLU284
CTHR314
CHOH517
CHOH537
CHOH563
CHOH606
CHOH667

site_idAC4
Number of Residues25
Detailsbinding site for residue LJS D 401
ChainResidue
DHOH539
DHOH562
DHOH567
DHOH569
DPHE58
DLYS59
DSER82
DTHR83
DASN85
DTHR86
DPHE132
DASN152
DSER153
DARG158
DVAL184
DGLY185
DASN186
DALA187
DGLY188
DASN189
DALA237
DILE240
DGLU284
DTHR314
DHOH522

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Egvnp.TGSFKDRGM
ChainResidueDetails
AGLU50-MET63

223166

PDB entries from 2024-07-31

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