Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1P5J

Crystal Structure Analysis of Human Serine Dehydratase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003941molecular_functionL-serine ammonia-lyase activity
A0004794molecular_functionthreonine deaminase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0006094biological_processgluconeogenesis
A0006520biological_processamino acid metabolic process
A0006565biological_processL-serine catabolic process
A0006629biological_processlipid metabolic process
A0016829molecular_functionlyase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042803molecular_functionprotein homodimerization activity
A0042866biological_processpyruvate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 941
ChainResidue
APHE40
ALEU172
AALA269
ACYS303
AGLY304
AGLY305
AHOH418
AHOH420
ALYS41
AASN67
ASER166
AVAL167
AGLY168
AGLY169
AGLY170
AGLY171

Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Dsaqp.SGSFKIRGI
ChainResidueDetails
AASP32-ILE45

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:16580895
ChainResidueDetails
APRO128

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:15689518
ChainResidueDetails
ALYS41

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pwh
ChainResidueDetails
ALYS41

234440

PDB entries from 2025-04-09

PDB statisticsPDBj update infoContact PDBjnumon