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6TI3

Apo-SHMT from Streptococcus thermophilus Tyr55Ser variant in complex with D-Threonine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
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
B0003824molecular_functioncatalytic activity
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
C0003824molecular_functioncatalytic activity
C0004372molecular_functionglycine hydroxymethyltransferase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006545biological_processglycine biosynthetic process
C0006565biological_processL-serine catabolic process
C0006730biological_processone-carbon metabolic process
C0008270molecular_functionzinc ion binding
C0008652biological_processamino acid biosynthetic process
C0016740molecular_functiontransferase activity
C0019264biological_processglycine biosynthetic process from serine
C0030170molecular_functionpyridoxal phosphate binding
C0035999biological_processtetrahydrofolate interconversion
C0046653biological_processtetrahydrofolate metabolic process
C0046655biological_processfolic acid metabolic process
C0050897molecular_functioncobalt ion binding
C0070905molecular_functionserine binding
D0003824molecular_functioncatalytic activity
D0004372molecular_functionglycine hydroxymethyltransferase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006545biological_processglycine biosynthetic process
D0006565biological_processL-serine catabolic process
D0006730biological_processone-carbon metabolic process
D0008270molecular_functionzinc ion binding
D0008652biological_processamino acid biosynthetic process
D0016740molecular_functiontransferase activity
D0019264biological_processglycine biosynthetic process from serine
D0030170molecular_functionpyridoxal phosphate binding
D0035999biological_processtetrahydrofolate interconversion
D0046653biological_processtetrahydrofolate metabolic process
D0046655biological_processfolic acid metabolic process
D0050897molecular_functioncobalt ion binding
D0070905molecular_functionserine binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue GOL A 501
ChainResidue
ATYR156
AASP183
AHOH625
AHOH626
AHOH708
AHOH708

site_idAC2
Number of Residues13
Detailsbinding site for residue DTH A 502
ChainResidue
ATHR227
AHIS229
ALYS230
AHOH690
AHOH699
CGLU57
CGLY261
CGLY262
CHOH675
CHOH706
ASER97
AGLY98
ASER99

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL C 501
ChainResidue
BLEU153
BARG180
BHOH687
BHOH719
CASP183
CHOH624
CHOH652

site_idAC4
Number of Residues11
Detailsbinding site for residue DTH C 502
ChainResidue
AGLU57
AGLY261
AGLY262
AHOH737
CSER97
CGLY98
CSER99
CTHR227
CHIS229
CLYS230
CHOH608

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL B 501
ChainResidue
BTYR156
BASP183
BHOH610
BHOH613
BHOH666
BHOH687
BHOH719
BHOH750
CARG180

site_idAC6
Number of Residues10
Detailsbinding site for residue DTH B 502
ChainResidue
BSER97
BGLY98
BSER99
BTHR227
BHIS229
BLYS230
BHOH679
BHOH722
DGLU57
DGLY262

site_idAC7
Number of Residues6
Detailsbinding site for residue NA D 501
ChainResidue
DALA203
DALA206
DHIS229
DLYS230
DTHR231
DLEU232

site_idAC8
Number of Residues10
Detailsbinding site for residue DTH D 502
ChainResidue
BGLU57
BGLY261
BGLY262
BHOH710
DSER97
DGLY98
DSER99
DHIS229
DLYS230
DHOH646

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVtTTTTHKTLrGPRGG
ChainResidueDetails
AHIS222-GLY238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALEU121
AGLY125
ASER355
CLEU121
CGLY125
CSER355
BLEU121
BGLY125
BSER355
DLEU121
DGLY125
DSER355

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
AHIS229
CHIS229
BHIS229
DHIS229

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALYS230
CLYS230
BLYS230
DLYS230

221051

PDB entries from 2024-06-12

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