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

6SLH

Conformational flexibility within the small domain of human serine racemase.

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000166molecular_functionnucleotide binding
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
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
AAA1901986biological_processresponse to ketamine
BBB0000166molecular_functionnucleotide binding
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
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
BBB1901986biological_processresponse to ketamine
CCC0000166molecular_functionnucleotide binding
CCC0000287molecular_functionmagnesium ion binding
CCC0003824molecular_functioncatalytic activity
CCC0003941molecular_functionL-serine ammonia-lyase activity
CCC0005509molecular_functioncalcium ion binding
CCC0005515molecular_functionprotein binding
CCC0005524molecular_functionATP binding
CCC0005737cellular_componentcytoplasm
CCC0005829cellular_componentcytosol
CCC0006520biological_processamino acid metabolic process
CCC0006563biological_processL-serine metabolic process
CCC0008721molecular_functionD-serine ammonia-lyase activity
CCC0009069biological_processserine family amino acid metabolic process
CCC0009410biological_processresponse to xenobiotic stimulus
CCC0016594molecular_functionglycine binding
CCC0016829molecular_functionlyase activity
CCC0016853molecular_functionisomerase activity
CCC0018114molecular_functionthreonine racemase activity
CCC0030165molecular_functionPDZ domain binding
CCC0030170molecular_functionpyridoxal phosphate binding
CCC0030378molecular_functionserine racemase activity
CCC0032496biological_processresponse to lipopolysaccharide
CCC0042802molecular_functionidentical protein binding
CCC0042803molecular_functionprotein homodimerization activity
CCC0042866biological_processpyruvate biosynthetic process
CCC0043025cellular_componentneuronal cell body
CCC0045177cellular_componentapical part of cell
CCC0046872molecular_functionmetal ion binding
CCC0070178biological_processD-serine metabolic process
CCC0070179biological_processD-serine biosynthetic process
CCC1901986biological_processresponse to ketamine
DDD0000166molecular_functionnucleotide binding
DDD0000287molecular_functionmagnesium ion binding
DDD0003824molecular_functioncatalytic activity
DDD0003941molecular_functionL-serine ammonia-lyase activity
DDD0005509molecular_functioncalcium ion binding
DDD0005515molecular_functionprotein binding
DDD0005524molecular_functionATP binding
DDD0005737cellular_componentcytoplasm
DDD0005829cellular_componentcytosol
DDD0006520biological_processamino acid metabolic process
DDD0006563biological_processL-serine metabolic process
DDD0008721molecular_functionD-serine ammonia-lyase activity
DDD0009069biological_processserine family amino acid metabolic process
DDD0009410biological_processresponse to xenobiotic stimulus
DDD0016594molecular_functionglycine binding
DDD0016829molecular_functionlyase activity
DDD0016853molecular_functionisomerase activity
DDD0018114molecular_functionthreonine racemase activity
DDD0030165molecular_functionPDZ domain binding
DDD0030170molecular_functionpyridoxal phosphate binding
DDD0030378molecular_functionserine racemase activity
DDD0032496biological_processresponse to lipopolysaccharide
DDD0042802molecular_functionidentical protein binding
DDD0042803molecular_functionprotein homodimerization activity
DDD0042866biological_processpyruvate biosynthetic process
DDD0043025cellular_componentneuronal cell body
DDD0045177cellular_componentapical part of cell
DDD0046872molecular_functionmetal ion binding
DDD0070178biological_processD-serine metabolic process
DDD0070179biological_processD-serine biosynthetic process
DDD1901986biological_processresponse to ketamine
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 Residues8
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"O59791","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35410329","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NBH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35410329","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ZSP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35410329","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NBC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35410329","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NBD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20106978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29277459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35410329","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3L6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5X2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q76EQ0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32039887","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35410329","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6SLH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ZUJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20106978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35410329","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3L6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L6R","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20106978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3L6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3L6R","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35410329","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NBC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"20106978","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29277459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35410329","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3L6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5X2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7NBG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"Q9QZX7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

PDB statisticsPDBj update infoContact PDBjnumon