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6TI4

SHMT from Streptococcus thermophilus Tyr55Ser variant in complex with PLP/D-Serine/Lys230 gem diamine complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0006545biological_processglycine biosynthetic process
A0006730biological_processone-carbon metabolic process
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
C0003824molecular_functioncatalytic activity
C0004372molecular_functionglycine hydroxymethyltransferase activity
C0005737cellular_componentcytoplasm
C0006545biological_processglycine biosynthetic process
C0006730biological_processone-carbon metabolic process
C0008652biological_processamino acid biosynthetic process
C0016740molecular_functiontransferase activity
C0019264biological_processglycine biosynthetic process from serine
C0030170molecular_functionpyridoxal phosphate binding
C0035999biological_processtetrahydrofolate interconversion
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue GOL A 501
ChainResidue
ATYR156
AARG180
AASP183
AHOH663
AHOH664
AHOH664
AHOH676
AHOH692
AHOH758

site_idAC2
Number of Residues20
Detailsbinding site for residue O3Z A 502
ChainResidue
ASER35
ASER97
AGLY98
ASER99
AHIS126
ASER176
AASP201
AALA203
AHIS204
AHIS229
ALYS230
AARG363
AHOH703
AHOH760
CGLU57
CTYR65
CGLY261
CGLY262
CHOH717
CHOH758

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL A 503
ChainResidue
AHIS213
APRO219
AGLU288
AILE291
ALYS292
AHOH601
AHOH783

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 504
ChainResidue
ASER55
AALA56
AGLU57
AARG63
ATYR64
ATYR65

site_idAC5
Number of Residues25
Detailsbinding site for Di-peptide O3Z C 501 and LYS C 230
ChainResidue
AGLU57
ATYR65
AGLY261
AGLY262
AHOH723
CSER35
CASN37
CSER97
CGLY98
CSER99
CHIS126
CSER176
CASP201
CALA203
CHIS204
CHIS229
CTHR231
CLEU232
CARG233
CARG363
CHOH653
CHOH673
CHOH691
CHOH704
CHOH745

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 Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALEU121
AGLY125
ASER355
CLEU121
CGLY125
CSER355

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
AHIS229
CHIS229

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALYS230
CLYS230

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PDB entries from 2024-07-10

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