Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3R0X

Crystal structure of Selenomethionine incorporated apo D-serine deaminase from Salmonella tyhimurium

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 Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 449
ChainResidue
AASN238
ASER239
AARG240
ATHR241
AHOH485
AHOH777
AHOH789

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 450
ChainResidue
AGLY413
AHOH458
AHOH760
AHOH787
AASN98
AGLY99

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 451
ChainResidue
ATYR11

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 452
ChainResidue
AALA390
AARG394
AHOH482

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 453
ChainResidue
AASN27
AGLY29
AGLU352
AARG353
AHOH578

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 454
ChainResidue
ACYS276
AGLY277
AGLU303
ASER307
ACYS309
ALEU338
AVAL340

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 455
ChainResidue
ALYS116
AGLY277
AVAL278
AGLY279
AGLY280
AGLY281
APRO282
AHOH831
AHOH835
AHOH841

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 456
ChainResidue
AHIS51

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE EDO A 457
ChainResidue
ALYS116
ASER165
ATHR166
AGLY167
AASN168
ALEU169
AASP236
AHOH834
AHOH841

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

225158

PDB entries from 2024-09-18

PDB statisticsPDBj update infoContact PDBjnumon