4QF5
Crystal structure I of MurF from Acinetobacter baumannii
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 | 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 | 0046872 | molecular_function | metal ion binding |
| A | 0047480 | molecular_function | UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine 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 | 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 | 0046872 | molecular_function | metal ion binding |
| B | 0047480 | molecular_function | UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP A 501 |
| Chain | Residue |
| A | SER123 |
| A | ASN296 |
| A | ARG327 |
| A | LEU328 |
| A | ASP341 |
| A | ASN344 |
| A | SER349 |
| A | LYS448 |
| A | MG502 |
| A | MG503 |
| A | GLY124 |
| A | LYS125 |
| A | THR126 |
| A | THR127 |
| A | ASN150 |
| A | GLU172 |
| A | ASN197 |
| A | HIS292 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 502 |
| Chain | Residue |
| A | THR126 |
| A | ASN150 |
| A | GLU172 |
| A | ATP501 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | HIS202 |
| A | KCX216 |
| A | ATP501 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP B 501 |
| Chain | Residue |
| B | SER123 |
| B | GLY124 |
| B | LYS125 |
| B | THR126 |
| B | THR127 |
| B | ASN150 |
| B | GLU172 |
| B | ASN197 |
| B | HIS292 |
| B | ASN296 |
| B | ARG327 |
| B | ASP341 |
| B | ASN344 |
| B | SER349 |
| B | ALA352 |
| B | LYS448 |
| B | MG502 |
| B | MG503 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| B | THR126 |
| B | ASN150 |
| B | GLU172 |
| B | ATP501 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 503 |
| Chain | Residue |
| B | HIS202 |
| B | KCX216 |
| B | ATP501 |
