4P3M
Crystal structure of serine hydroxymethyltransferase from Psychromonas ingrahamii
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 L-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 L-serine |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0035999 | biological_process | tetrahydrofolate interconversion |
| B | 0046653 | biological_process | tetrahydrofolate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | ILE33 |
| A | ALA34 |
| A | SER35 |
| A | ASN345 |
| A | ARG363 |
| A | HOH694 |
| A | HOH801 |
| B | TYR65 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | GLY98 |
| A | SER99 |
| A | THR227 |
| A | HIS229 |
| A | HOH715 |
| A | HOH752 |
| B | TYR55 |
| B | GLY262 |
| B | GLY263 |
| A | SER97 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | TYR55 |
| A | GLY263 |
| A | HOH754 |
| B | SER97 |
| B | GLY98 |
| B | SER99 |
| B | THR227 |
| B | HIS229 |
| B | LYS230 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | ARG81 |
| A | HOH670 |
| A | HOH783 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 505 |
| Chain | Residue |
| A | THR227 |
| A | HIS229 |
| A | LYS230 |
| A | THR231 |
| A | LEU232 |
| A | HOH653 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 506 |
| Chain | Residue |
| A | ARG42 |
| B | MET6 |
| B | ASN7 |
| B | HOH826 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 507 |
| Chain | Residue |
| A | ASN7 |
| B | ARG42 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 508 |
| Chain | Residue |
| A | TYR59 |
| A | ILE79 |
| A | ALA91 |
| A | ASN92 |
| A | ASN253 |
| A | HOH644 |
| A | HOH735 |
| A | HOH753 |
| A | HOH789 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 509 |
| Chain | Residue |
| A | PRO215 |
| A | GLN378 |
| A | HOH607 |
| A | HOH616 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 510 |
| Chain | Residue |
| A | ALA280 |
| A | ASP388 |
| A | ALA405 |
| A | VAL406 |
| A | LYS409 |
| A | HOH612 |
| A | HOH615 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 511 |
| Chain | Residue |
| A | LYS398 |
| A | LEU399 |
| A | ALA400 |
| A | THR401 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| A | TYR65 |
| B | ILE33 |
| B | ALA34 |
| B | SER35 |
| B | ARG363 |
| B | HOH689 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | LEU232 |
| B | GLY233 |
| B | GLU278 |
| B | CYS279 |
| B | ARG371 |
| B | HOH688 |
| B | HOH805 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | VAL209 |
| B | ASN216 |
| B | HOH632 |
| B | HOH726 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | ILE79 |
| B | ALA91 |
| B | ASN92 |
| B | ASN253 |
| B | HOH677 |
| B | HOH681 |
Functional Information from PROSITE/UniProt
| site_id | PS00096 |
| Number of Residues | 17 |
| Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DVvTTTTHKTLgGPRGG |
| Chain | Residue | Details |
| A | ASP222-GLY238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Site: {"description":"Plays an important role in substrate specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
