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6LUT

Crystal structure of Serine Racemase from Dictyostelium discoideum.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0003941molecular_functionL-serine ammonia-lyase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006563biological_processL-serine metabolic process
A0006565biological_processL-serine catabolic process
A0008721molecular_functionD-serine ammonia-lyase activity
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0018114molecular_functionthreonine racemase activity
A0030170molecular_functionpyridoxal phosphate binding
A0030378molecular_functionserine racemase activity
A0036088biological_processD-serine catabolic process
A0042866biological_processpyruvate biosynthetic process
A0046872molecular_functionmetal ion binding
A0070179biological_processD-serine biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0003941molecular_functionL-serine ammonia-lyase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006563biological_processL-serine metabolic process
B0006565biological_processL-serine catabolic process
B0008721molecular_functionD-serine ammonia-lyase activity
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0018114molecular_functionthreonine racemase activity
B0030170molecular_functionpyridoxal phosphate binding
B0030378molecular_functionserine racemase activity
B0036088biological_processD-serine catabolic process
B0042866biological_processpyruvate biosynthetic process
B0046872molecular_functionmetal ion binding
B0070179biological_processD-serine biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O59791
ChainResidueDetails
ALLP56
ASER81
BLLP56
BSER81

site_idSWS_FT_FI2
Number of Residues36
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9GZT4
ChainResidueDetails
ASER32
AGLY183
AGLY184
AGLY185
AGLU207
AALA211
AASP213
ALYS277
ASER310
AASN313
BSER32
ALYS51
BLYS51
BTHR52
BTHR78
BASN83
BGLN86
BTYR118
BASP175
BGLY182
BGLY183
BGLY184
ATHR52
BGLY185
BGLU207
BALA211
BASP213
BLYS277
BSER310
BASN313
ATHR78
AASN83
AGLN86
ATYR118
AASP175
AGLY182

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q9GZT4
ChainResidueDetails
ALLP56
BLLP56

227344

PDB entries from 2024-11-13

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