Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6HYY

Human phosphoserine phosphatase with serine and phosphate

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
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
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 Residues10
Detailsbinding site for residue PO4 A 301
ChainResidue
AMET52
AHOH453
AGLY53
AGLY180
AALA181
ATHR182
AARG202
AHOH404
AHOH417
AHOH419

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 302
ChainResidue
AASP20
AASP22
AASP179
AHOH453
AHOH455
AHOH515

site_idAC3
Number of Residues12
Detailsbinding site for residue SER A 303
ChainResidue
AASP20
AVAL21
AASP22
AILE108
ASER109
AGLY110
ALYS158
AHOH401
AHOH402
AHOH404
AHOH446
AHOH515

site_idAC4
Number of Residues11
Detailsbinding site for residue PO4 B 301
ChainResidue
BASP20
BVAL21
BASP22
BSER109
BGLY110
BGLY111
BLYS158
BCA302
BHOH417
BHOH461
BHOH501

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 302
ChainResidue
BASP20
BASP22
BASP179
BPO4301
BHOH435
BHOH521

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J
ChainResidueDetails
AASP20
BASP20

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J
ChainResidueDetails
AASP22
BASP22

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYY
ChainResidueDetails
AASP20
AASP22
AASP179
BASP20
BASP22
BASP179

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:31205021, ECO:0007744|PDB:6HYJ, ECO:0007744|PDB:6HYY, ECO:0007744|PDB:6Q6J
ChainResidueDetails
AMET52
BTHR182
AGLY53
ASER109
ALYS158
ATHR182
BMET52
BGLY53
BSER109
BLYS158

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon