7Q8E
Crystal Structure of the MurT-GatD Enzyme Complex from Staphylococcus aureus COL strain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| A | 0016881 | molecular_function | acid-amino acid ligase activity |
| A | 0140282 | molecular_function | carbon-nitrogen ligase activity on lipid II |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0009236 | biological_process | cobalamin biosynthetic process |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0071555 | biological_process | cell wall organization |
| B | 0140282 | molecular_function | carbon-nitrogen ligase activity on lipid II |
| C | 0005524 | molecular_function | ATP binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016874 | molecular_function | ligase activity |
| C | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| C | 0016881 | molecular_function | acid-amino acid ligase activity |
| C | 0140282 | molecular_function | carbon-nitrogen ligase activity on lipid II |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004359 | molecular_function | glutaminase activity |
| D | 0009236 | biological_process | cobalamin biosynthetic process |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0071555 | biological_process | cell wall organization |
| D | 0140282 | molecular_function | carbon-nitrogen ligase activity on lipid II |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3JUU7","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_02214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3JUU7","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_02214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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_FI4 |
| 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_FI5 |
| 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_FI6 |
| 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 |
