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6HYJ

PSPH Human phosphoserine phosphatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001701biological_processin utero embryonic development
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
B0001701biological_processin utero embryonic development
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 Residues14
Detailsbinding site for residue SEP A 301
ChainResidue
AASP20
AHOH408
AHOH413
AHOH416
AHOH422
AHOH439
AMET52
AGLY53
ASER109
AGLY110
ALYS158
ATHR182
AHOH401
AHOH403

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 302
ChainResidue
AASP20
AASP22
AASP179
AHOH416
AHOH422
AHOH424

site_idAC3
Number of Residues4
Detailsbinding site for residue SEP B 301
ChainResidue
BPHE131
BPRO151
BLYS168
BHOH401

site_idAC4
Number of Residues6
Detailsbinding site for residue CA B 302
ChainResidue
BASP20
BASP22
BASP179
BHOH420
BHOH459
BHOH467

site_idAC5
Number of Residues5
Detailsbinding site for residue SER B 303
ChainResidue
AGLN203
ALYS206
AASP207
BGLU29
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

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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