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6ZSP

Human serine racemase bound to ATP and malonate.

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000287molecular_functionmagnesium ion binding
AAA0003824molecular_functioncatalytic activity
AAA0003941molecular_functionL-serine ammonia-lyase activity
AAA0005509molecular_functioncalcium ion binding
AAA0005515molecular_functionprotein binding
AAA0005524molecular_functionATP binding
AAA0005737cellular_componentcytoplasm
AAA0005829cellular_componentcytosol
AAA0006520biological_processamino acid metabolic process
AAA0006563biological_processL-serine metabolic process
AAA0008721molecular_functionD-serine ammonia-lyase activity
AAA0009069biological_processserine family amino acid metabolic process
AAA0009410biological_processresponse to xenobiotic stimulus
AAA0014070biological_processresponse to organic cyclic compound
AAA0016594molecular_functionglycine binding
AAA0016829molecular_functionlyase activity
AAA0016853molecular_functionisomerase activity
AAA0018114molecular_functionthreonine racemase activity
AAA0030165molecular_functionPDZ domain binding
AAA0030170molecular_functionpyridoxal phosphate binding
AAA0030378molecular_functionserine racemase activity
AAA0032496biological_processresponse to lipopolysaccharide
AAA0042802molecular_functionidentical protein binding
AAA0042803molecular_functionprotein homodimerization activity
AAA0042866biological_processpyruvate biosynthetic process
AAA0043025cellular_componentneuronal cell body
AAA0045177cellular_componentapical part of cell
AAA0046872molecular_functionmetal ion binding
AAA0070178biological_processD-serine metabolic process
AAA0070179biological_processD-serine biosynthetic process
BBB0000287molecular_functionmagnesium ion binding
BBB0003824molecular_functioncatalytic activity
BBB0003941molecular_functionL-serine ammonia-lyase activity
BBB0005509molecular_functioncalcium ion binding
BBB0005515molecular_functionprotein binding
BBB0005524molecular_functionATP binding
BBB0005737cellular_componentcytoplasm
BBB0005829cellular_componentcytosol
BBB0006520biological_processamino acid metabolic process
BBB0006563biological_processL-serine metabolic process
BBB0008721molecular_functionD-serine ammonia-lyase activity
BBB0009069biological_processserine family amino acid metabolic process
BBB0009410biological_processresponse to xenobiotic stimulus
BBB0014070biological_processresponse to organic cyclic compound
BBB0016594molecular_functionglycine binding
BBB0016829molecular_functionlyase activity
BBB0016853molecular_functionisomerase activity
BBB0018114molecular_functionthreonine racemase activity
BBB0030165molecular_functionPDZ domain binding
BBB0030170molecular_functionpyridoxal phosphate binding
BBB0030378molecular_functionserine racemase activity
BBB0032496biological_processresponse to lipopolysaccharide
BBB0042802molecular_functionidentical protein binding
BBB0042803molecular_functionprotein homodimerization activity
BBB0042866biological_processpyruvate biosynthetic process
BBB0043025cellular_componentneuronal cell body
BBB0045177cellular_componentapical part of cell
BBB0046872molecular_functionmetal ion binding
BBB0070178biological_processD-serine metabolic process
BBB0070179biological_processD-serine biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00165
Number of Residues14
DetailsDEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. Elfqk.TGSFKIRGA
ChainResidueDetails
AAAGLU47-ALA60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:O59791
ChainResidueDetails
AAALLP56
AAASER84
BBBLLP56
BBBSER84

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:7NBH
ChainResidueDetails
AAAGLU13
BBBGLU13

site_idSWS_FT_FI3
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:6ZSP
ChainResidueDetails
AAASER31
BBBSER31
BBBSER32
BBBILE33
BBBLYS51
BBBTHR52
BBBGLN89
BBBTYR121
BBBLYS279
BBBASN316
AAASER32
AAAILE33
AAALYS51
AAATHR52
AAAGLN89
AAATYR121
AAALYS279
AAAASN316

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:7NBC, ECO:0007744|PDB:7NBF
ChainResidueDetails
AAAPRO69
BBBPRO69

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:7NBD
ChainResidueDetails
AAATHR81
BBBTHR81

site_idSWS_FT_FI6
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:20106978, ECO:0000269|PubMed:29277459, ECO:0000269|PubMed:35410329, ECO:0007744|PDB:3L6B, ECO:0007744|PDB:5X2L, ECO:0007744|PDB:7NBC, ECO:0007744|PDB:7NBD, ECO:0007744|PDB:7NBF, ECO:0007744|PDB:7NBG
ChainResidueDetails
AAAASN86
BBBGLY186
BBBGLY187
BBBGLY188
BBBMET189
BBBSER313
AAAGLY185
AAAGLY186
AAAGLY187
AAAGLY188
AAAMET189
AAASER313
BBBASN86
BBBGLY185

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q76EQ0
ChainResidueDetails
AAAASN154
BBBASN154

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:32039887, ECO:0000269|PubMed:35410329, ECO:0007744|PDB:6SLH, ECO:0007744|PDB:6ZUJ, ECO:0007744|PDB:7NBD
ChainResidueDetails
AAAASP178
BBBASP178

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20106978, ECO:0000269|PubMed:35410329, ECO:0007744|PDB:3L6B, ECO:0007744|PDB:3L6R
ChainResidueDetails
AAAGLU210
BBBGLU210

site_idSWS_FT_FI10
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20106978, ECO:0007744|PDB:3L6B, ECO:0007744|PDB:3L6R
ChainResidueDetails
AAAALA214
AAAASP216
BBBALA214
BBBASP216

site_idSWS_FT_FI11
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:35410329, ECO:0007744|PDB:7NBC, ECO:0007744|PDB:7NBD, ECO:0007744|PDB:7NBF, ECO:0007744|PDB:7NBG, ECO:0007744|PDB:7NBH
ChainResidueDetails
AAAASN247
BBBASN247

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20106978, ECO:0000269|PubMed:29277459, ECO:0000269|PubMed:35410329, ECO:0007744|PDB:3L6B, ECO:0007744|PDB:5X2L, ECO:0007744|PDB:7NBC, ECO:0007744|PDB:7NBD, ECO:0007744|PDB:7NBF, ECO:0007744|PDB:7NBG
ChainResidueDetails
AAALLP56
BBBLLP56

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q9QZX7
ChainResidueDetails
AAACYS113
BBBCYS113

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PDB entries from 2024-07-10

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