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3SS7

Crystal structure of holo D-serine dehydratase from Escherichia coli at 1.55 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
X0005737cellular_componentcytoplasm
X0005829cellular_componentcytosol
X0006520biological_processamino acid metabolic process
X0006974biological_processDNA damage response
X0008721molecular_functionD-serine ammonia-lyase activity
X0009097biological_processisoleucine biosynthetic process
X0016829molecular_functionlyase activity
X0016836molecular_functionhydro-lyase activity
X0030170molecular_functionpyridoxal phosphate binding
X0036088biological_processD-serine catabolic process
X0046416biological_processD-amino acid metabolic process
X0051410biological_processdetoxification of nitrogen compound
X0070178biological_processD-serine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL X 501
ChainResidue
XALA392
XARG396
XHOH699
XHOH943
XHOH1030

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP X 502
ChainResidue
XGLY281
XGLY282
XGLY283
XPRO284
XLEU340
XGLU384
XTHR424
XHOH781
XHOH884
XHOH993
XHOH997
XLYS118
XASN170
XGLY279
XVAL280

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K X 503
ChainResidue
XCYS278
XGLY279
XGLU305
XSER309
XCYS311
XHOH854

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues15
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. DshlpiSGSIKARGG
ChainResidueDetails
XASP108-GLY122

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:22197591, ECO:0007744|PDB:3SS7, ECO:0007744|PDB:3SS9
ChainResidueDetails
XLYS118

218853

PDB entries from 2024-04-24

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