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4J5U

X-ray crystal structure of a serine hydroxymethyltransferase with covalently bound PLP from Rickettsia rickettsii str. Sheila Smith

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006545biological_processglycine biosynthetic process
A0006565biological_processL-serine catabolic process
A0006730biological_processone-carbon metabolic process
A0008270molecular_functionzinc ion binding
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
A0046653biological_processtetrahydrofolate metabolic process
A0046655biological_processfolic acid metabolic process
A0050897molecular_functioncobalt ion binding
A0070905molecular_functionserine binding
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006545biological_processglycine biosynthetic process
B0006565biological_processL-serine catabolic process
B0006730biological_processone-carbon metabolic process
B0008270molecular_functionzinc ion binding
B0008652biological_processamino acid biosynthetic process
B0016740molecular_functiontransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0035999biological_processtetrahydrofolate interconversion
B0046653biological_processtetrahydrofolate metabolic process
B0046655biological_processfolic acid metabolic process
B0050897molecular_functioncobalt ion binding
B0070905molecular_functionserine binding
Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HAvTSTTHKTLrGPRGG
ChainResidueDetails
AHIS222-GLY238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALEU121
AGLY125
AGLU246
ASER354
BLEU121
BGLY125
BGLU246
BSER354

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
AHIS229
BHIS229

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALLP230
BLLP230

220472

PDB entries from 2024-05-29

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