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3IAU

The structure of the processed form of threonine deaminase isoform 2 from Solanum lycopersicum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004794molecular_functionthreonine deaminase activity
A0006520biological_processamino acid metabolic process
A0009097biological_processisoleucine biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0004794molecular_functionthreonine deaminase activity
B0006520biological_processamino acid metabolic process
B0009097biological_processisoleucine biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 367
ChainResidue
ALYS84
BHOH505
AASN312
AHOH446
AHOH447
AHOH494
AHOH714
BLYS84
BASN312
BHOH484

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 15P A 368
ChainResidue
AHIS210
ALYS237
ATYR328
APHE331
ATYR332
AHOH428

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 369
ChainResidue
ASER115
AALA116
AGLY117
APHE164
AACT370

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 370
ChainResidue
ALLP91
AHIS119
APRO185
AACT369
AHOH670

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT B 367
ChainResidue
BSER115
BALA116
BPHE164
BHOH415
BHOH694

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Edkqr.VFSFKLRGA
ChainResidueDetails
AGLU82-ALA95

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:P04968
ChainResidueDetails
ALLP91
BLLP91

218853

PDB entries from 2024-04-24

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