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6UXL

Structure of serine hydroxymethyltransferase 8 from Glycine max cultivar Forrest complexed with PLP-Glycine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0006730biological_processone-carbon metabolic process
A0008168molecular_functionmethyltransferase activity
A0009507cellular_componentchloroplast
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0032259biological_processmethylation
A0035999biological_processtetrahydrofolate interconversion
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0006730biological_processone-carbon metabolic process
B0008168molecular_functionmethyltransferase activity
B0009507cellular_componentchloroplast
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0032259biological_processmethylation
B0035999biological_processtetrahydrofolate interconversion
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue PLG A 501
ChainResidue
ASER39
AHIS218
ATHR241
AHIS243
ALYS244
AARG389
BTYR59
BTYR69
BGLY289
BGLY290
ASER105
AGLY106
ASER107
AHIS134
AGLY189
ASER190
AASP215
AALA217

site_idAC2
Number of Residues20
Detailsbinding site for residue PLG B 501
ChainResidue
ATYR59
AGLU61
ATYR69
ATYR104
AGLY289
AGLY290
BSER39
BSER105
BGLY106
BSER107
BHIS134
BGLY189
BSER190
BASP215
BALA217
BHIS218
BTHR241
BHIS243
BLYS244
BARG389

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DIvTTTTHKSLrGPRAG
ChainResidueDetails
AASP236-GLY252

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PDB entries from 2024-09-11

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