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1V7C

Crystal structure of threonine synthase from thermus thermophilus hb8 in complex with a substrate analogue

Replaces:  1UIQ
Functional Information from GO Data
ChainGOidnamespacecontents
A0004795molecular_functionthreonine synthase activity
A0005737cellular_componentcytoplasm
A0006520biological_processamino acid metabolic 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
B0005737cellular_componentcytoplasm
B0006520biological_processamino acid metabolic process
B0009088biological_processthreonine biosynthetic process
B0016829molecular_functionlyase activity
B0019344biological_processcysteine biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B1901605biological_processalpha-amino acid metabolic process
C0004795molecular_functionthreonine synthase activity
C0005737cellular_componentcytoplasm
C0006520biological_processamino acid metabolic process
C0009088biological_processthreonine biosynthetic process
C0016829molecular_functionlyase activity
C0019344biological_processcysteine biosynthetic process
C0030170molecular_functionpyridoxal phosphate binding
C1901605biological_processalpha-amino acid metabolic process
D0004795molecular_functionthreonine synthase activity
D0005737cellular_componentcytoplasm
D0006520biological_processamino acid metabolic process
D0009088biological_processthreonine biosynthetic process
D0016829molecular_functionlyase activity
D0019344biological_processcysteine biosynthetic process
D0030170molecular_functionpyridoxal phosphate binding
D1901605biological_processalpha-amino acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEY A 1400
ChainResidue
APHE60
AARG160
AVAL186
AGLY187
AASN188
AALA189
AGLY190
AASN191
AALA240
AILE241
AGLU287
ALYS61
ATHR317
AHOH1402
AHOH1406
AHOH1427
AHOH1441
AHOH1465
ASER84
ATHR85
AASN87
ATHR88
APHE134
AASN154
ASER155

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEY B 2400
ChainResidue
BPHE60
BLYS61
BSER84
BTHR85
BASN87
BTHR88
BPHE134
BASN154
BSER155
BARG160
BVAL186
BGLY187
BASN188
BALA189
BGLY190
BASN191
BALA240
BILE241
BGLU287
BTHR317
BHOH2402
BHOH2403
BHOH2413
BHOH2422
BHOH2514

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEY C 3400
ChainResidue
CPHE60
CLYS61
CSER84
CTHR85
CASN87
CTHR88
CPHE134
CASN154
CSER155
CARG160
CPRO185
CVAL186
CGLY187
CASN188
CALA189
CGLY190
CASN191
CALA240
CILE241
CGLU287
CTHR317
CHOH3408
CHOH3416
CHOH3449
CHOH3462
CHOH3512

site_idAC4
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEY D 4400
ChainResidue
DHOH4448
DHOH4581
DPHE60
DLYS61
DSER84
DTHR85
DASN87
DTHR88
DPHE134
DASN154
DSER155
DARG160
DVAL186
DGLY187
DASN188
DALA189
DGLY190
DASN191
DALA240
DILE241
DGLU287
DTHR317
DHOH4401
DHOH4414
DHOH4442

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Eglnp.TGSFKDRGM
ChainResidueDetails
AGLU52-MET65

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PDB entries from 2024-06-12

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