6GS2
Crystal Structure of the GatD/MurT Enzyme Complex from Staphylococcus aureus
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 | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| B | 0016881 | molecular_function | acid-amino acid ligase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| B | 0140282 | molecular_function | carbon-nitrogen ligase activity on lipid II |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004359 | molecular_function | glutaminase activity |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0009236 | biological_process | cobalamin biosynthetic process |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016874 | molecular_function | ligase activity |
| C | 0071555 | biological_process | cell wall organization |
| C | 0140282 | molecular_function | carbon-nitrogen ligase activity on lipid II |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| D | 0016881 | molecular_function | acid-amino acid ligase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071555 | biological_process | cell wall organization |
| D | 0140282 | molecular_function | carbon-nitrogen ligase activity on lipid II |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue 144 A 301 |
| Chain | Residue |
| A | ASP138 |
| A | HOH468 |
| A | HOH492 |
| C | ASP138 |
| C | THR139 |
| C | THR159 |
| A | THR139 |
| A | GLY158 |
| A | THR159 |
| A | HIS179 |
| A | HOH409 |
| A | HOH410 |
| A | HOH421 |
| A | HOH443 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 302 |
| Chain | Residue |
| A | ILE213 |
| A | PRO214 |
| B | SER239 |
| B | ASP241 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| B | CYS202 |
| B | CYS205 |
| B | CYS224 |
| B | CYS226 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | HIS189 |
| B | ASP262 |
| B | HOH610 |
| B | HOH634 |
| B | HOH689 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| D | CYS202 |
| D | CYS205 |
| D | CYS224 |
| D | CYS226 |
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":"22291598","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"30154570","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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H2WZ38","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_02213","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30154570","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02214","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30154570","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
