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8SSJ

Room-temperature X-ray structure of human mitochondrial serine hydroxymethyltransferase (hSHMT2)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002082biological_processregulation of oxidative phosphorylation
A0003682molecular_functionchromatin binding
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005743cellular_componentmitochondrial inner membrane
A0005759cellular_componentmitochondrial matrix
A0006544biological_processglycine metabolic process
A0006545biological_processglycine biosynthetic process
A0006563biological_processL-serine metabolic process
A0006564biological_processL-serine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0008284biological_processpositive regulation of cell population proliferation
A0008732molecular_functionL-allo-threonine aldolase activity
A0015630cellular_componentmicrotubule cytoskeleton
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0034340biological_processresponse to type I interferon
A0035999biological_processtetrahydrofolate interconversion
A0042645cellular_componentmitochondrial nucleoid
A0042802molecular_functionidentical protein binding
A0046653biological_processtetrahydrofolate metabolic process
A0051262biological_processprotein tetramerization
A0051289biological_processprotein homotetramerization
A0070062cellular_componentextracellular exosome
A0070129biological_processregulation of mitochondrial translation
A0070536biological_processprotein K63-linked deubiquitination
A0070552cellular_componentBRISC complex
A1903715biological_processregulation of aerobic respiration
B0002082biological_processregulation of oxidative phosphorylation
B0003682molecular_functionchromatin binding
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005743cellular_componentmitochondrial inner membrane
B0005759cellular_componentmitochondrial matrix
B0006544biological_processglycine metabolic process
B0006545biological_processglycine biosynthetic process
B0006563biological_processL-serine metabolic process
B0006564biological_processL-serine biosynthetic process
B0006730biological_processone-carbon metabolic process
B0008284biological_processpositive regulation of cell population proliferation
B0008732molecular_functionL-allo-threonine aldolase activity
B0015630cellular_componentmicrotubule cytoskeleton
B0016597molecular_functionamino acid binding
B0016740molecular_functiontransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0034340biological_processresponse to type I interferon
B0035999biological_processtetrahydrofolate interconversion
B0042645cellular_componentmitochondrial nucleoid
B0042802molecular_functionidentical protein binding
B0046653biological_processtetrahydrofolate metabolic process
B0051262biological_processprotein tetramerization
B0051289biological_processprotein homotetramerization
B0070062cellular_componentextracellular exosome
B0070129biological_processregulation of mitochondrial translation
B0070536biological_processprotein K63-linked deubiquitination
B0070552cellular_componentBRISC complex
B1903715biological_processregulation of aerobic respiration
Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DIvTTTTHKTLrGARSG
ChainResidueDetails
AASP272-GLY288

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS103
ALYS181
ALYS196
ALYS297
ALYS356
ALYS464
ALYS469
ALYS474
BLYS103
BLYS181
BLYS196
BLYS297
BLYS356
BLYS464
BLYS469
BLYS474

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:29180469
ChainResidueDetails
ALLP280
BLLP280

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER470
BSER470

221051

PDB entries from 2024-06-12

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