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4H27

Modulating the function of human serine racemase and human serine dehydratase by protein engineering

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
A0006567biological_processthreonine catabolic process
A0006629biological_processlipid metabolic process
A0009097biological_processisoleucine biosynthetic 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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AVAL225
ALYS226
ATHR227
AHOH623
AHOH624
AHOH954

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AASN67
AALA68
AHOH629
AHOH840
AHOH949
AHOH952
ALLP41
ASER64
AGLY66

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ATYR132
APRO134
APRO135
AHOH519
AHOH553
AHOH735
AHOH760
AHOH761
AHOH762
AHOH763
AHOH827
AHOH839

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
ALLP41

224201

PDB entries from 2024-08-28

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