6H5E
Crystal Structure of the GatD/MurT Enzyme Complex from Staphylococcus aureus with bound AMPPNP
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 | 4 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| B | CYS202 |
| B | CYS205 |
| B | CYS224 |
| B | CYS226 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue ANP B 502 |
| Chain | Residue |
| B | THR61 |
| B | ASN85 |
| B | GLU108 |
| B | ASN130 |
| B | PHE132 |
| B | TYR216 |
| B | PHE263 |
| B | ASN267 |
| B | MG503 |
| B | HOH601 |
| B | HOH609 |
| B | HOH613 |
| B | HOH622 |
| B | HOH623 |
| D | MET136 |
| D | ASP137 |
| D | ARG138 |
| B | THR56 |
| B | ASN57 |
| B | GLY58 |
| B | LYS59 |
| B | THR60 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | THR60 |
| B | GLU108 |
| B | ANP502 |
| B | HOH613 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue 144 C 301 |
| Chain | Residue |
| A | ASP138 |
| A | THR139 |
| A | THR159 |
| C | ASP138 |
| C | THR159 |
| C | HOH401 |
| C | HOH424 |
| C | HOH430 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 302 |
| Chain | Residue |
| C | ASN127 |
| C | ARG128 |
| C | ARG152 |
| C | ASP171 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| C | GLY166 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL C 304 |
| Chain | Residue |
| C | GLU209 |
| C | ILE213 |
| C | PRO214 |
| C | PHE215 |
| C | LYS218 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue PEG C 305 |
| Chain | Residue |
| C | ASP221 |
| C | GLU223 |
| C | ALA224 |
| C | GLN227 |
| D | GLN380 |
| D | LYS384 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| D | CYS202 |
| D | CYS205 |
| D | CYS224 |
| D | CYS226 |
| site_id | AD1 |
| Number of Residues | 23 |
| Details | binding site for residue ANP D 502 |
| Chain | Residue |
| B | MET136 |
| B | ASP137 |
| B | ARG138 |
| D | THR56 |
| D | ASN57 |
| D | GLY58 |
| D | LYS59 |
| D | THR60 |
| D | THR61 |
| D | ASN85 |
| D | GLU108 |
| D | ASN130 |
| D | PHE132 |
| D | TYR216 |
| D | PHE263 |
| D | ASN267 |
| D | MG503 |
| D | HOH601 |
| D | HOH602 |
| D | HOH604 |
| D | HOH614 |
| D | HOH623 |
| D | HOH630 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 503 |
| Chain | Residue |
| D | THR60 |
| D | GLU108 |
| D | ANP502 |
| D | HOH604 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL D 504 |
| Chain | Residue |
| B | ASN204 |
| D | GLY347 |
| D | ARG348 |
| D | ASP349 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL D 505 |
| Chain | Residue |
| D | GLU151 |
| D | SER154 |
| D | ASN155 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue PEG D 506 |
| Chain | Residue |
| D | HIS221 |
| D | TYR222 |
| D | ARG230 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue PEG D 507 |
| Chain | Residue |
| D | ASP397 |
| D | ILE398 |
| D | TYR399 |
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_FI6 |
| 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_FI7 |
| 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 |
