6MTG
A Single Reactive Noncanonical Amino Acid is Able to Dramatically Stabilize Protein Structure
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004414 | molecular_function | homoserine O-acetyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008899 | molecular_function | homoserine O-succinyltransferase activity |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0019281 | biological_process | L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0004414 | molecular_function | homoserine O-acetyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008899 | molecular_function | homoserine O-succinyltransferase activity |
B | 0009086 | biological_process | methionine biosynthetic process |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0019281 | biological_process | L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine |
B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue PEG A 401 |
Chain | Residue |
A | ALA82 |
A | HOH561 |
B | LEU152 |
B | TYR153 |
B | GLY154 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue PEG A 402 |
Chain | Residue |
A | HOH548 |
A | HOH564 |
A | HOH704 |
B | ARG56 |
B | SER59 |
B | ASN60 |
B | HOH604 |
A | GLU18 |
A | VAL20 |
A | HIS176 |
A | ARG181 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue FMT A 403 |
Chain | Residue |
A | ALA177 |
A | LEU178 |
A | LEU179 |
A | TYR292 |
A | HOH624 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue FMT A 404 |
Chain | Residue |
A | LEU255 |
A | ASP256 |
A | HOH513 |
B | LYS47 |
B | ARG78 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue GOL B 401 |
Chain | Residue |
B | LEU173 |
B | HIS174 |
B | GLU209 |
B | ILE210 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue FMT B 402 |
Chain | Residue |
B | ALA177 |
B | LEU178 |
B | LEU179 |
B | TYR292 |
B | HOH555 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue FMT B 403 |
Chain | Residue |
B | GLY107 |
B | ALA108 |
B | CSD142 |
B | TRP143 |
B | HIS235 |
B | HOH591 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue FMT B 404 |
Chain | Residue |
A | GLN158 |
B | GLU8 |
B | ASP117 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Acyl-thioester intermediate => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:10572016, ECO:0000305|PubMed:17302437, ECO:0000305|PubMed:17442255 |
Chain | Residue | Details |
A | CSD142 | |
B | CSD142 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:17302437, ECO:0000305|PubMed:17442255 |
Chain | Residue | Details |
A | HIS235 | |
B | HIS235 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305|PubMed:17302437, ECO:0000305|PubMed:17442255 |
Chain | Residue | Details |
A | GLU237 | |
B | GLU237 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00295 |
Chain | Residue | Details |
A | LYS163 | |
A | SER192 | |
A | ARG249 | |
B | LYS163 | |
B | SER192 | |
B | ARG249 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Important for acyl-CoA specificity => ECO:0000255|HAMAP-Rule:MF_00295 |
Chain | Residue | Details |
A | GLY111 | |
B | GLY111 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_00295 |
Chain | Residue | Details |
A | SER192 | |
B | SER192 |