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4F4F

X-Ray crystal structure of PLP bound Threonine synthase from Brucella melitensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004795molecular_functionthreonine synthase activity
A0006520biological_processamino acid metabolic process
A0009088biological_processthreonine biosynthetic process
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
B0004795molecular_functionthreonine synthase activity
B0006520biological_processamino acid metabolic process
B0009088biological_processthreonine biosynthetic process
B0016829molecular_functionlyase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP A 501
ChainResidue
APHE111
ASER307
AHIS386
ATHR409
AALA410
AHOH765
AHOH795
AHOH812
AHOH924
ALYS112
APRO253
ATHR254
AGLY255
AASN256
APHE257
AGLY258
AASP259

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP B 501
ChainResidue
BPHE111
BLYS112
BPRO253
BTHR254
BGLY255
BASN256
BPHE257
BGLY258
BASP259
BSER307
BHIS386
BTHR409
BALA410
BHOH669
BHOH718

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues15
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. ElfhgpTLAFKDVAM
ChainResidueDetails
AGLU102-MET116

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PDB entries from 2024-08-28

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