1Y7M
Crystal Structure of the B. subtilis YkuD protein at 2 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018104 | biological_process | peptidoglycan-protein cross-linking |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| A | 0031160 | cellular_component | spore wall |
| A | 0071555 | biological_process | cell wall organization |
| A | 0071972 | molecular_function | peptidoglycan L,D-transpeptidase activity |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018104 | biological_process | peptidoglycan-protein cross-linking |
| B | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0031160 | cellular_component | spore wall |
| B | 0071555 | biological_process | cell wall organization |
| B | 0071972 | molecular_function | peptidoglycan L,D-transpeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 201 |
| Chain | Residue |
| A | CYS139 |
| A | SO4203 |
| A | HOH204 |
| B | HIS119 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 202 |
| Chain | Residue |
| A | HIS119 |
| B | CYS139 |
| B | SO4204 |
| B | HOH207 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 203 |
| Chain | Residue |
| A | SER136 |
| A | LYS137 |
| A | GLY138 |
| A | CYS139 |
| A | ARG141 |
| A | CD201 |
| B | HIS119 |
| A | HIS123 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 204 |
| Chain | Residue |
| A | HIS119 |
| B | HIS123 |
| B | SER136 |
| B | LYS137 |
| B | GLY138 |
| B | CYS139 |
| B | ARG141 |
| B | CD202 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 205 |
| Chain | Residue |
| A | ARG159 |
| A | HOH238 |
| B | TYR96 |
| B | ARG159 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 206 |
| Chain | Residue |
| A | ASN144 |
| B | LYS145 |
| B | HOH211 |
| B | HOH225 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01373 |
| Chain | Residue | Details |
| A | HIS123 | |
| B | HIS123 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01373 |
| Chain | Residue | Details |
| A | CYS139 | |
| B | CYS139 |
