6G80
Structure of Mycobacterium hassiacum MeT1 from orthorhombic crystals.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0030206 | biological_process | chondroitin sulfate biosynthetic process |
A | 0032259 | biological_process | methylation |
A | 0046872 | molecular_function | metal ion binding |
A | 0071770 | biological_process | DIM/DIP cell wall layer assembly |
B | 0005886 | cellular_component | plasma membrane |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0030206 | biological_process | chondroitin sulfate biosynthetic process |
B | 0032259 | biological_process | methylation |
B | 0046872 | molecular_function | metal ion binding |
B | 0071770 | biological_process | DIM/DIP cell wall layer assembly |
C | 0005886 | cellular_component | plasma membrane |
C | 0008168 | molecular_function | methyltransferase activity |
C | 0030206 | biological_process | chondroitin sulfate biosynthetic process |
C | 0032259 | biological_process | methylation |
C | 0046872 | molecular_function | metal ion binding |
C | 0071770 | biological_process | DIM/DIP cell wall layer assembly |
M | 0005886 | cellular_component | plasma membrane |
M | 0008168 | molecular_function | methyltransferase activity |
M | 0030206 | biological_process | chondroitin sulfate biosynthetic process |
M | 0032259 | biological_process | methylation |
M | 0046872 | molecular_function | metal ion binding |
M | 0071770 | biological_process | DIM/DIP cell wall layer assembly |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue SAH A 301 |
Chain | Residue |
A | GLY19 |
A | GLY122 |
A | SER124 |
A | ASP141 |
A | GLY142 |
A | GLY143 |
A | ARG151 |
A | HOH410 |
B | HIS229 |
A | MET21 |
A | GLU44 |
A | GLY46 |
A | TYR48 |
A | SER52 |
A | ASP71 |
A | HIS72 |
A | GLY75 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL B 301 |
Chain | Residue |
B | ARG188 |
B | ASN191 |
B | THR192 |
B | LEU218 |
B | LYS219 |
B | HOH411 |
site_id | AC3 |
Number of Residues | 21 |
Details | binding site for residue SAH M 301 |
Chain | Residue |
M | GLY19 |
M | PHE20 |
M | GLU44 |
M | GLY46 |
M | TYR48 |
M | LYS51 |
M | SER52 |
M | ASP71 |
M | HIS72 |
M | GLY75 |
M | SER76 |
M | GLY122 |
M | LYS123 |
M | SER124 |
M | ASP141 |
M | GLY142 |
M | GLY143 |
M | ARG151 |
M | HOH405 |
M | HOH406 |
M | HOH426 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue SAH C 301 |
Chain | Residue |
C | GLY19 |
C | PHE20 |
C | GLY46 |
C | TYR48 |
C | SER52 |
C | ASP71 |
C | HIS72 |
C | GLY75 |
C | SER76 |
C | GLY122 |
C | SER124 |
C | ASP141 |
C | GLY142 |
C | GLY143 |
C | HOH409 |
C | HOH413 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:30606802 |
Chain | Residue | Details |
A | HIS144 | |
B | HIS144 | |
M | HIS144 | |
C | HIS144 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000305|PubMed:30606802 |
Chain | Residue | Details |
A | PHE20 | |
B | SER52 | |
B | ASP71 | |
B | GLY75 | |
B | SER124 | |
B | ARG151 | |
M | PHE20 | |
M | GLY46 | |
M | SER52 | |
M | ASP71 | |
M | GLY75 | |
A | GLY46 | |
M | SER124 | |
M | ARG151 | |
C | PHE20 | |
C | GLY46 | |
C | SER52 | |
C | ASP71 | |
C | GLY75 | |
C | SER124 | |
C | ARG151 | |
A | SER52 | |
A | ASP71 | |
A | GLY75 | |
A | SER124 | |
A | ARG151 | |
B | PHE20 | |
B | GLY46 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:30606802 |
Chain | Residue | Details |
A | ASP141 | |
C | ASP141 | |
C | HIS169 | |
C | ASP170 | |
A | HIS169 | |
A | ASP170 | |
B | ASP141 | |
B | HIS169 | |
B | ASP170 | |
M | ASP141 | |
M | HIS169 | |
M | ASP170 |