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3R0Z

Crystal structure of apo D-serine deaminase from Salmonella typhimurium

Functional Information from GO Data
ChainGOidnamespacecontents
A0006520biological_processamino acid metabolic process
A0008721molecular_functionD-serine ammonia-lyase activity
A0009097biological_processisoleucine biosynthetic process
A0016829molecular_functionlyase activity
A0016836molecular_functionhydro-lyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0036088biological_processD-serine catabolic process
A0046416biological_processD-amino acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 449
ChainResidue
ALYS116
AGLY277
AVAL278
AGLY279
AGLY280
AGLY281
APRO282
AHOH499

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 450
ChainResidue
AGLY345
APHE346
AHOH474
ASER344

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 451
ChainResidue
ALYS116
AGLY167
AASN168
AGLY337
AHOH455
AHOH473
AHOH499
AHOH588

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 452
ChainResidue
ALYS105
AHIS108
AGLY378
AARG380

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 453
ChainResidue
ASER239
AARG240
ATHR241

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues15
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. DshlaiSGSIKARGG
ChainResidueDetails
AASP106-GLY120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01030
ChainResidueDetails
ALYS116

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PDB entries from 2024-07-24

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