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6UXI

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0035999biological_processtetrahydrofolate interconversion
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue PLG A 701
ChainResidue
ASER39
AHIS218
ATHR241
AHIS243
ALYS244
AARG389
BTYR59
BTYR104
BGLY289
BGLY290
BHOH959
ASER105
AGLY106
ASER107
AHIS134
AGLY189
ASER190
AASP215
AALA217

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 702
ChainResidue
AILE48
AGLU49
AGLY52
AHOH819
BGLY52
BHOH973

site_idAC3
Number of Residues18
Detailsbinding site for residue PLG B 801
ChainResidue
ATYR59
AGLY289
AGLY290
BSER39
BSER105
BGLY106
BSER107
BHIS134
BGLY189
BSER190
BASP215
BALA217
BHIS218
BTHR241
BHIS243
BLYS244
BARG389
BHOH984

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO B 802
ChainResidue
ALYS176
AASP179
BLYS176
BASP179

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

221716

PDB entries from 2024-06-26

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