5N9M
Crystal structure of GatD - a glutamine amidotransferase from Staphylococcus aureus involved in peptidoglycan amidation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009236 | biological_process | cobalamin biosynthetic process |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0071555 | biological_process | cell wall organization |
| A | 0140282 | molecular_function | carbon-nitrogen ligase activity on lipid II |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009236 | biological_process | cobalamin biosynthetic process |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0071555 | biological_process | cell wall organization |
| B | 0140282 | molecular_function | carbon-nitrogen ligase activity on lipid II |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue GLN A 301 |
| Chain | Residue |
| A | TYR17 |
| B | ARG235 |
| B | ARG238 |
| A | ARG128 |
| A | HOH402 |
| A | HOH414 |
| A | HOH450 |
| A | HOH459 |
| A | HOH502 |
| A | HOH547 |
| A | HOH549 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue PG4 A 302 |
| Chain | Residue |
| A | GLU85 |
| A | GLY87 |
| A | LYS181 |
| A | HOH406 |
| A | HOH545 |
| B | GLU85 |
| B | LYS181 |
| B | ASN182 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 382 |
| Details | Domain: {"description":"GATase cobBQ-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00606","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_02213","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00606","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29593310","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02213","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00606","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29593310","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02213","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29593310","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
