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1L8L

Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006563biological_processL-serine metabolic process
A0006564biological_processL-serine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0009612biological_processresponse to mechanical stimulus
A0016787molecular_functionhydrolase activity
A0031667biological_processresponse to nutrient levels
A0033574biological_processresponse to testosterone
A0036424molecular_functionL-phosphoserine phosphatase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006563biological_processL-serine metabolic process
B0006564biological_processL-serine biosynthetic process
B0008652biological_processamino acid biosynthetic process
B0009612biological_processresponse to mechanical stimulus
B0016787molecular_functionhydrolase activity
B0031667biological_processresponse to nutrient levels
B0033574biological_processresponse to testosterone
B0036424molecular_functionL-phosphoserine phosphatase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE APO A 800
ChainResidue
AASP20
AASP22
AGLU29
ASER109
AGLY110
ALYS158
AASP179
AGLY180
ATHR182

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE APO B 801
ChainResidue
BASP20
BVAL21
BASP22
BSER109
BGLY110
BLYS158
BTHR182
BASP183
BARG202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"31205021","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6HYJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HYY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q6J","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"31205021","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6HYJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HYY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q6J","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31205021","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HYJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6HYY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6Q6J","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"31205021","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HYY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
ASER109
ALYS160

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lvh
ChainResidueDetails
BSER109
BLYS160

247947

PDB entries from 2026-01-21

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