6YMD
Crystal structure of serine hydroxymethyltransferase from Aphanothece halophytica in the covalent complex with malonate
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 | 0006544 | biological_process | glycine metabolic process |
A | 0006545 | biological_process | glycine biosynthetic process |
A | 0006563 | biological_process | L-serine metabolic process |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0008168 | molecular_function | methyltransferase activity |
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 | 0032259 | biological_process | methylation |
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 | 0006544 | biological_process | glycine metabolic process |
B | 0006545 | biological_process | glycine biosynthetic process |
B | 0006563 | biological_process | L-serine metabolic process |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0008168 | molecular_function | methyltransferase activity |
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 | 0032259 | biological_process | methylation |
B | 0035999 | biological_process | tetrahydrofolate interconversion |
B | 0046653 | biological_process | tetrahydrofolate metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | PRO42 |
A | TYR416 |
A | HOH818 |
A | HOH873 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | PRO133 |
A | HIS145 |
A | GLN332 |
A | HOH982 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue NA A 505 |
Chain | Residue |
A | LEU323 |
A | VAL326 |
A | LEU328 |
A | HOH800 |
A | HOH831 |
A | GLU142 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | GLN21 |
B | GLN25 |
B | HOH635 |
B | HOH728 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
B | LYS170 |
B | GLY196 |
B | HOH676 |
B | HOH740 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO B 505 |
Chain | Residue |
B | LEU86 |
B | VAL210 |
B | ALA211 |
B | GLN404 |
B | HOH601 |
B | HOH602 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue NA B 506 |
Chain | Residue |
B | GLY138 |
B | PHE141 |
B | HOH830 |
B | HOH857 |
B | HOH878 |
B | HOH969 |
site_id | AC8 |
Number of Residues | 22 |
Details | binding site for residues PMP A 501 and MLI B 501 |
Chain | Residue |
A | SER36 |
A | SER98 |
A | GLY99 |
A | ALA100 |
A | HIS127 |
A | SER177 |
A | ASP202 |
A | ALA204 |
A | HIS205 |
A | THR228 |
A | HIS230 |
A | LYS231 |
A | ARG363 |
A | HOH655 |
A | HOH664 |
A | HOH811 |
B | TYR56 |
B | GLU58 |
B | TYR66 |
B | GLY262 |
B | GLY263 |
B | HOH646 |
site_id | AC9 |
Number of Residues | 30 |
Details | binding site for residues MLI A 504 and PMP B 502 |
Chain | Residue |
A | PRO42 |
A | TYR56 |
A | GLU58 |
A | TYR66 |
A | GLY262 |
A | GLY263 |
A | TYR416 |
A | HOH614 |
A | HOH818 |
A | HOH873 |
B | SER36 |
B | SER98 |
B | GLY99 |
B | ALA100 |
B | HIS127 |
B | LYS170 |
B | SER177 |
B | GLY196 |
B | ASP202 |
B | ALA204 |
B | HIS205 |
B | THR228 |
B | HIS230 |
B | LYS231 |
B | ARG363 |
B | HOH655 |
B | HOH676 |
B | HOH737 |
B | HOH740 |
B | HOH820 |
site_id | AD1 |
Number of Residues | 24 |
Details | binding site for Di-peptide PMP B 502 and LYS B 231 |
Chain | Residue |
B | HIS205 |
B | THR228 |
B | HIS230 |
B | THR232 |
B | LEU233 |
B | ARG234 |
B | HOH655 |
B | HOH699 |
B | HOH737 |
B | HOH820 |
B | HOH835 |
A | TYR56 |
A | GLY262 |
A | GLY263 |
A | MLI504 |
B | SER36 |
B | ASN38 |
B | SER98 |
B | GLY99 |
B | ALA100 |
B | HIS127 |
B | SER177 |
B | ASP202 |
B | ALA204 |
Functional Information from PROSITE/UniProt
site_id | PS00096 |
Number of Residues | 17 |
Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DVvTTTTHKTLrGPRGG |
Chain | Residue | Details |
A | ASP223-GLY239 |