Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7QX8

Crystal structure of serine hydroxymethyltransferase, isoform 7 from Arabidopsis thaliana (SHM7)

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
C0004372molecular_functionglycine hydroxymethyltransferase activity
C0019264biological_processglycine biosynthetic process from serine
C0030170molecular_functionpyridoxal phosphate binding
C0035999biological_processtetrahydrofolate interconversion
D0004372molecular_functionglycine hydroxymethyltransferase activity
D0019264biological_processglycine biosynthetic process from serine
D0030170molecular_functionpyridoxal phosphate binding
D0035999biological_processtetrahydrofolate interconversion
E0004372molecular_functionglycine hydroxymethyltransferase activity
E0019264biological_processglycine biosynthetic process from serine
E0030170molecular_functionpyridoxal phosphate binding
E0035999biological_processtetrahydrofolate interconversion
F0004372molecular_functionglycine hydroxymethyltransferase activity
F0019264biological_processglycine biosynthetic process from serine
F0030170molecular_functionpyridoxal phosphate binding
F0035999biological_processtetrahydrofolate interconversion
G0004372molecular_functionglycine hydroxymethyltransferase activity
G0019264biological_processglycine biosynthetic process from serine
G0030170molecular_functionpyridoxal phosphate binding
G0035999biological_processtetrahydrofolate interconversion
H0004372molecular_functionglycine hydroxymethyltransferase activity
H0019264biological_processglycine biosynthetic process from serine
H0030170molecular_functionpyridoxal phosphate binding
H0035999biological_processtetrahydrofolate interconversion
I0004372molecular_functionglycine hydroxymethyltransferase activity
I0019264biological_processglycine biosynthetic process from serine
I0030170molecular_functionpyridoxal phosphate binding
I0035999biological_processtetrahydrofolate interconversion
J0004372molecular_functionglycine hydroxymethyltransferase activity
J0019264biological_processglycine biosynthetic process from serine
J0030170molecular_functionpyridoxal phosphate binding
J0035999biological_processtetrahydrofolate interconversion
K0004372molecular_functionglycine hydroxymethyltransferase activity
K0019264biological_processglycine biosynthetic process from serine
K0030170molecular_functionpyridoxal phosphate binding
K0035999biological_processtetrahydrofolate interconversion
L0004372molecular_functionglycine hydroxymethyltransferase activity
L0019264biological_processglycine biosynthetic process from serine
L0030170molecular_functionpyridoxal phosphate binding
L0035999biological_processtetrahydrofolate interconversion
Functional Information from PROSITE/UniProt
site_idPS00096
Number of Residues17
DetailsSHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DIvTSTTHKGLrGPRGG
ChainResidueDetails
AASP362-GLY378

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVTGgtDnHLLLWDL
ChainResidueDetails
ALEU467-LEU481

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS370
BLYS370
CLYS370
DLYS370
ELYS370
FLYS370
GLYS370
HLYS370
ILYS370
JLYS370
KLYS370
LLYS370

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon