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 | 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 |
B | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
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 |
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 | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051 |
Chain | Residue | Details |
A | LEU116 | |
A | GLY120 | |
A | GLU240 | |
A | SER348 | |
B | LEU116 | |
B | GLY120 | |
B | GLU240 | |
B | SER348 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051 |
Chain | Residue | Details |
A | HIS223 | |
B | HIS223 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051 |
Chain | Residue | Details |
A | LYS224 | |
B | LYS224 |