7U35
Crystal Structure of UDP-N-acetylmuramoylalanine--D-glutamate ligase (MurD) from Pseudomonas aeruginosa PAO1 in complex with ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0008360 | biological_process | regulation of cell shape |
A | 0008764 | molecular_function | UDP-N-acetylmuramoylalanine-D-glutamate ligase activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0016881 | molecular_function | acid-amino acid ligase activity |
A | 0051301 | biological_process | cell division |
A | 0071555 | biological_process | cell wall organization |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0008360 | biological_process | regulation of cell shape |
B | 0008764 | molecular_function | UDP-N-acetylmuramoylalanine-D-glutamate ligase activity |
B | 0009058 | biological_process | biosynthetic process |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0016881 | molecular_function | acid-amino acid ligase activity |
B | 0051301 | biological_process | cell division |
B | 0071555 | biological_process | cell wall organization |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0008360 | biological_process | regulation of cell shape |
C | 0008764 | molecular_function | UDP-N-acetylmuramoylalanine-D-glutamate ligase activity |
C | 0009058 | biological_process | biosynthetic process |
C | 0009252 | biological_process | peptidoglycan biosynthetic process |
C | 0016874 | molecular_function | ligase activity |
C | 0016881 | molecular_function | acid-amino acid ligase activity |
C | 0051301 | biological_process | cell division |
C | 0071555 | biological_process | cell wall organization |
Functional Information from PROSITE/UniProt
site_id | PS00012 |
Number of Residues | 16 |
Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. GSNAKSTVTTLVGEMA |
Chain | Residue | Details |
A | GLY116-ALA131 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 19 |
Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2022","submissionDatabase":"PDB data bank","title":"Crystal Structure of UDP-N-acetylmuramoylalanine--D-glutamate ligase (MurD) from Pseudomonas aeruginosa PAO1 in complex with UMA (Uridine-5'-diphosphate-N-acetylmuramoyl-L-Alanine).","authoringGroup":["Seattle structural genomics center for infectious disease (SSGCID)"]}},{"source":"PDB","id":"7U35","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00639","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 24 |
Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2022","submissionDatabase":"PDB data bank","title":"Crystal structure of UDP-N-acetylmuramoylalanine--D-glutamate ligase (MurD) from Pseudomonas aeruginosa PAO1 in complex with ADP.","authoringGroup":["Seattle structural genomics center for infectious disease (SSGCID)"]}},{"source":"PDB","id":"7U35","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |