3N0L
Crystal structure of serine hydroxymethyltransferase from Campylobacter jejuni
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SO4 A 415 |
| Chain | Residue |
| A | SER92 |
| B | TYR50 |
| B | GLY255 |
| B | GLY256 |
| A | GLY93 |
| A | SER94 |
| A | THR221 |
| A | ARG230 |
| A | SO4416 |
| A | HOH570 |
| A | HOH599 |
| A | HOH614 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 416 |
| Chain | Residue |
| A | THR221 |
| A | HIS223 |
| A | LYS224 |
| A | ARG230 |
| A | GLY231 |
| A | SO4415 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 417 |
| Chain | Residue |
| A | SER30 |
| A | SER170 |
| A | HIS198 |
| A | LYS224 |
| A | ARG356 |
| B | TYR50 |
| B | TYR60 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 418 |
| Chain | Residue |
| A | ASN-1 |
| A | ALA0 |
| A | MSE1 |
| A | SER2 |
| B | GLU40 |
| B | ARG411 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 419 |
| Chain | Residue |
| A | VAL342 |
| A | PRO343 |
| A | GLY344 |
| A | GLU345 |
| A | HOH494 |
| A | HOH656 |
| B | LYS370 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 420 |
| Chain | Residue |
| A | LYS78 |
| A | ASN82 |
| A | CYS83 |
| A | LYS84 |
| A | HOH501 |
| B | HOH460 |
| B | HOH539 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 421 |
| Chain | Residue |
| A | CYS22 |
| A | PHE33 |
| A | ARG365 |
| A | PHE406 |
| A | ILE407 |
| A | ILE408 |
| A | TYR409 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 422 |
| Chain | Residue |
| A | ASP318 |
| A | ARG319 |
| A | GLU320 |
| A | PHE321 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SO4 B 415 |
| Chain | Residue |
| A | TYR50 |
| A | GLY255 |
| A | GLY256 |
| B | SER92 |
| B | GLY93 |
| B | SER94 |
| B | ARG230 |
| B | SO4416 |
| B | HOH550 |
| B | HOH572 |
| B | HOH628 |
| B | HOH629 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 416 |
| Chain | Residue |
| B | THR221 |
| B | HIS223 |
| B | LYS224 |
| B | ARG230 |
| B | GLY231 |
| B | SO4415 |
| B | HOH540 |
| B | HOH550 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 417 |
| Chain | Residue |
| A | TYR50 |
| A | TYR60 |
| B | SER30 |
| B | SER170 |
| B | HIS198 |
| B | LYS224 |
| B | ARG356 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 418 |
| Chain | Residue |
| B | ARG174 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 419 |
| Chain | Residue |
| B | LEU35 |
| B | GLU37 |
| B | PHE271 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 420 |
| Chain | Residue |
| A | GLU40 |
| A | ARG411 |
| B | ALA0 |
| B | MSE1 |
| B | SER2 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 421 |
| Chain | Residue |
| A | ASP186 |
| A | HOH571 |
| B | ARG182 |
| B | ASP186 |
| B | HOH557 |
Functional Information from PROSITE/UniProt
| site_id | PS00096 |
| Number of Residues | 17 |
| Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVvSSTTHKTLrGPRGG |
| Chain | Residue | Details |
| A | HIS216-GLY232 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| 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 |
