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3H7F

Crystal structure of serine hydroxymethyltransferase from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004372molecular_functionglycine hydroxymethyltransferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006544biological_processglycine metabolic process
A0006545biological_processglycine biosynthetic process
A0006563biological_processL-serine metabolic process
A0006730biological_processone-carbon metabolic process
A0008652biological_processamino acid biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016740molecular_functiontransferase activity
A0019264biological_processglycine biosynthetic process from serine
A0030170molecular_functionpyridoxal phosphate binding
A0035999biological_processtetrahydrofolate interconversion
A0042783biological_processevasion of host immune response
A0042803molecular_functionprotein homodimerization activity
A0046653biological_processtetrahydrofolate metabolic process
B0004372molecular_functionglycine hydroxymethyltransferase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006544biological_processglycine metabolic process
B0006545biological_processglycine biosynthetic process
B0006563biological_processL-serine metabolic process
B0006730biological_processone-carbon metabolic process
B0008652biological_processamino acid biosynthetic process
B0009274cellular_componentpeptidoglycan-based cell wall
B0016740molecular_functiontransferase activity
B0019264biological_processglycine biosynthetic process from serine
B0030170molecular_functionpyridoxal phosphate binding
B0035999biological_processtetrahydrofolate interconversion
B0042783biological_processevasion of host immune response
B0042803molecular_functionprotein homodimerization activity
B0046653biological_processtetrahydrofolate metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 427
ChainResidue
BHOH567
BHOH582
BHOH643
BHOH748
BHOH980
BHOH981

Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DVvSTTVHKTLgGGRSG
ChainResidueDetails
AASP219-GLY235

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
ALEU130
AGLY134
BLEU130
BGLY134

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
AVAL238
BVAL238

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051
ChainResidueDetails
AGLY239
BGLY239

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
AGLU54
ATHR224

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
BGLU54
BTHR224

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
AHIS201

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
BHIS201

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
ACYS65

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dfo
ChainResidueDetails
BCYS65

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PDB entries from 2024-07-24

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