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 | 0006541 | biological_process | glutamine metabolic process |
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 | 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 | 0006541 | biological_process | glutamine metabolic process |
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 | 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 | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000305|PubMed:30154570 |
Chain | Residue | Details |
B | ASP349 | |
D | ASP349 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02214, ECO:0000269|PubMed:30154570 |
Chain | Residue | Details |
B | CYS202 | |
B | CYS205 | |
B | CYS224 | |
B | CYS226 | |
D | CYS202 | |
D | CYS205 | |
D | CYS224 | |
D | CYS226 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:A0A0H2WZ38, ECO:0000255|HAMAP-Rule:MF_02213 |
Chain | Residue | Details |
A | ARG128 | |
C | ARG128 |