3ECD
Crystal structure of serine hydroxymethyltransferase from Burkholderia pseudomallei
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006545 | biological_process | glycine biosynthetic process |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0019264 | biological_process | glycine biosynthetic process from serine |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0035999 | biological_process | tetrahydrofolate interconversion |
A | 0046653 | biological_process | tetrahydrofolate metabolic process |
B | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006545 | biological_process | glycine biosynthetic process |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0019264 | biological_process | glycine biosynthetic process from serine |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0035999 | biological_process | tetrahydrofolate interconversion |
B | 0046653 | biological_process | tetrahydrofolate metabolic process |
C | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006545 | biological_process | glycine biosynthetic process |
C | 0006730 | biological_process | one-carbon metabolic process |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0019264 | biological_process | glycine biosynthetic process from serine |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0035999 | biological_process | tetrahydrofolate interconversion |
C | 0046653 | biological_process | tetrahydrofolate metabolic process |
D | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006545 | biological_process | glycine biosynthetic process |
D | 0006730 | biological_process | one-carbon metabolic process |
D | 0008652 | biological_process | amino acid biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0019264 | biological_process | glycine biosynthetic process from serine |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0035999 | biological_process | tetrahydrofolate interconversion |
D | 0046653 | biological_process | tetrahydrofolate metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 425 |
Chain | Residue |
A | ARG237 |
A | ASP286 |
A | TYR290 |
A | THR374 |
A | HOH677 |
A | HOH682 |
D | ASN5 |
D | PHE7 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 425 |
Chain | Residue |
B | ASP286 |
B | TYR290 |
B | THR374 |
B | HOH565 |
B | HOH747 |
B | HOH748 |
C | ASN5 |
C | PHE7 |
B | ARG237 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 425 |
Chain | Residue |
B | ASN5 |
B | PHE7 |
C | ARG237 |
C | ASP286 |
C | TYR290 |
C | THR374 |
C | HOH888 |
C | HOH990 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL D 425 |
Chain | Residue |
A | ASN5 |
A | PHE7 |
D | ARG237 |
D | ASP286 |
D | TYR290 |
D | THR374 |
D | HOH513 |
D | HOH543 |
D | HOH654 |
Functional Information from PROSITE/UniProt
site_id | PS00096 |
Number of Residues | 17 |
Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVvTSTTHKTLrGPRGG |
Chain | Residue | Details |
A | HIS226-GLY242 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051 |
Chain | Residue | Details |
A | LEU125 | |
D | LEU125 | |
D | GLY129 | |
D | GLU250 | |
A | GLY129 | |
A | GLU250 | |
B | LEU125 | |
B | GLY129 | |
B | GLU250 | |
C | LEU125 | |
C | GLY129 | |
C | GLU250 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051 |
Chain | Residue | Details |
A | HIS233 | |
B | HIS233 | |
C | HIS233 | |
D | HIS233 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051 |
Chain | Residue | Details |
A | LYS234 | |
B | LYS234 | |
C | LYS234 | |
D | LYS234 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
A | GLU61 | |
A | THR231 | |
A | LYS234 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
B | GLU61 | |
B | THR231 | |
B | LYS234 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
C | GLU61 | |
C | THR231 | |
C | LYS234 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
D | THR231 | |
D | LYS234 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
A | HIS208 | |
A | LYS234 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
B | HIS208 | |
B | LYS234 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
C | HIS208 | |
C | LYS234 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
D | HIS208 | |
D | LYS234 |