6YMF
Crystal structure of serine hydroxymethyltransferase from Aphanothece halophytica in the PLP-Serine external aldimine state
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 | 0006565 | biological_process | L-serine catabolic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| 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 |
| A | 0046655 | biological_process | folic acid metabolic process |
| A | 0050897 | molecular_function | cobalt ion binding |
| A | 0070905 | molecular_function | serine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | SER41 |
| A | PRO42 |
| A | LEU415 |
| A | TYR416 |
| A | GOL502 |
| A | HOH606 |
| A | HOH656 |
| A | HOH669 |
| A | HOH703 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | GLU278 |
| A | GOL501 |
| A | HOH616 |
| A | HOH698 |
| A | HOH756 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | GLN77 |
| A | ASP81 |
| A | LYS84 |
| A | ARG305 |
| A | ASN384 |
| A | HOH618 |
| A | HOH785 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue PLS A 504 |
| Chain | Residue |
| A | SER36 |
| A | TYR56 |
| A | GLU58 |
| A | TYR66 |
| A | SER98 |
| A | GLY99 |
| A | ALA100 |
| A | HIS127 |
| A | SER177 |
| A | ASP202 |
| A | ALA204 |
| A | HIS205 |
| A | THR228 |
| A | HIS230 |
| A | LYS231 |
| A | GLY262 |
| A | GLY263 |
| A | ARG363 |
| A | HOH771 |
| A | HOH803 |
| A | HOH810 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | SER212 |
| A | GLY213 |
| A | GLN400 |
| A | GLN404 |
| A | HOH610 |
| A | HOH630 |
| A | HOH645 |
| A | HOH692 |
| A | HOH725 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue 1PE A 506 |
| Chain | Residue |
| A | TYR198 |
| A | LYS251 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 507 |
| Chain | Residue |
| A | GLY59 |
| A | LYS254 |
| A | PHE257 |
| A | HOH632 |
| A | HOH690 |
| A | HOH702 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 508 |
| Chain | Residue |
| A | ARG168 |
| A | PRO169 |
| A | LYS170 |
| A | HOH770 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 509 |
| Chain | Residue |
| A | GLY196 |
| A | ALA197 |
| A | HOH609 |
| A | HOH633 |
| A | HOH719 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 510 |
| Chain | Residue |
| A | TYR157 |
| A | ASP158 |
| A | ALA190 |
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 |
