6X9F
Pseudomonas aeruginosa MurC with AZ8074
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0008360 | biological_process | regulation of cell shape |
A | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine 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 | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0008360 | biological_process | regulation of cell shape |
B | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine 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 | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0008360 | biological_process | regulation of cell shape |
C | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine 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 |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0008360 | biological_process | regulation of cell shape |
D | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine ligase activity |
D | 0009058 | biological_process | biosynthetic process |
D | 0009252 | biological_process | peptidoglycan biosynthetic process |
D | 0016874 | molecular_function | ligase activity |
D | 0016881 | molecular_function | acid-amino acid ligase activity |
D | 0051301 | biological_process | cell division |
D | 0071555 | biological_process | cell wall organization |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0008360 | biological_process | regulation of cell shape |
E | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine ligase activity |
E | 0009058 | biological_process | biosynthetic process |
E | 0009252 | biological_process | peptidoglycan biosynthetic process |
E | 0016874 | molecular_function | ligase activity |
E | 0016881 | molecular_function | acid-amino acid ligase activity |
E | 0051301 | biological_process | cell division |
E | 0071555 | biological_process | cell wall organization |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0008360 | biological_process | regulation of cell shape |
F | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine ligase activity |
F | 0009058 | biological_process | biosynthetic process |
F | 0009252 | biological_process | peptidoglycan biosynthetic process |
F | 0016874 | molecular_function | ligase activity |
F | 0016881 | molecular_function | acid-amino acid ligase activity |
F | 0051301 | biological_process | cell division |
F | 0071555 | biological_process | cell wall organization |
G | 0005524 | molecular_function | ATP binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0008360 | biological_process | regulation of cell shape |
G | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine ligase activity |
G | 0009058 | biological_process | biosynthetic process |
G | 0009252 | biological_process | peptidoglycan biosynthetic process |
G | 0016874 | molecular_function | ligase activity |
G | 0016881 | molecular_function | acid-amino acid ligase activity |
G | 0051301 | biological_process | cell division |
G | 0071555 | biological_process | cell wall organization |
H | 0005524 | molecular_function | ATP binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0008360 | biological_process | regulation of cell shape |
H | 0008763 | molecular_function | UDP-N-acetylmuramate-L-alanine ligase activity |
H | 0009058 | biological_process | biosynthetic process |
H | 0009252 | biological_process | peptidoglycan biosynthetic process |
H | 0016874 | molecular_function | ligase activity |
H | 0016881 | molecular_function | acid-amino acid ligase activity |
H | 0051301 | biological_process | cell division |
H | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue UXP A 501 |
Chain | Residue |
A | HIS117 |
C | EDO502 |
A | GLY118 |
A | THR182 |
A | ASN183 |
A | CYS219 |
A | TYR239 |
A | HIS281 |
A | LEU284 |
A | ASN285 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | PRO266 |
A | VAL291 |
A | ASP295 |
A | HOH602 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | PRO96 |
A | GLU99 |
A | HIS173 |
G | HIS208 |
G | ARG234 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | ASP221 |
A | LEU280 |
A | LEU284 |
C | ASP222 |
C | PRO223 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | PRO270 |
A | LEU271 |
A | ASP272 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | ALA19 |
A | GLY20 |
A | CYS22 |
A | GLY23 |
A | LEU145 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue DMS A 507 |
Chain | Residue |
A | LEU135 |
A | ARG158 |
A | TYR159 |
A | GLU296 |
A | GLY297 |
A | ILE298 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue UXP B 501 |
Chain | Residue |
B | GLY118 |
B | THR182 |
B | ASN183 |
B | CYS219 |
B | TYR239 |
B | HIS281 |
B | LEU284 |
B | ASN285 |
H | HOH603 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | ARG108 |
B | ALA156 |
B | ARG158 |
B | HOH622 |
D | HOH629 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | PRO96 |
B | GLU99 |
E | HIS208 |
E | ARG234 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
B | HIS109 |
B | ARG158 |
B | TYR159 |
B | GLU296 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue EDO B 505 |
Chain | Residue |
B | ASP221 |
B | LEU280 |
B | LEU284 |
H | ILE184 |
H | ASP222 |
H | PRO223 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue EDO B 506 |
Chain | Residue |
B | PRO270 |
B | LEU271 |
B | ASP272 |
B | HOH625 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
B | ALA19 |
B | GLY23 |
B | ARG144 |
B | LEU145 |
B | HOH644 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue DMS B 508 |
Chain | Residue |
B | ARG226 |
B | THR238 |
B | ASP244 |
E | ARG91 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue DMS B 509 |
Chain | Residue |
B | LEU135 |
B | ARG158 |
B | GLU296 |
B | GLY297 |
B | HOH613 |
D | HOH645 |
site_id | AD8 |
Number of Residues | 2 |
Details | binding site for residue DMS B 510 |
Chain | Residue |
B | PRO93 |
B | VAL94 |
site_id | AD9 |
Number of Residues | 9 |
Details | binding site for residue DMS B 511 |
Chain | Residue |
B | VAL220 |
B | ASP221 |
B | PRO223 |
B | ARG226 |
H | VAL220 |
H | ASP221 |
H | PRO223 |
H | ARG226 |
H | HOH636 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue DMS B 512 |
Chain | Residue |
B | ARG9 |
B | LEU31 |
B | TYR33 |
site_id | AE2 |
Number of Residues | 10 |
Details | binding site for residue UXP C 501 |
Chain | Residue |
C | HIS117 |
C | GLY118 |
C | THR182 |
C | ASN183 |
C | CYS219 |
C | TYR239 |
C | HIS281 |
C | LEU284 |
C | ASN285 |
C | EDO502 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue EDO C 502 |
Chain | Residue |
A | PRO223 |
A | UXP501 |
C | ASP221 |
C | LEU280 |
C | LEU284 |
C | UXP501 |
site_id | AE4 |
Number of Residues | 7 |
Details | binding site for residue EDO C 503 |
Chain | Residue |
A | VAL220 |
A | ASP221 |
A | ARG226 |
A | HOH654 |
C | VAL220 |
C | ASP221 |
C | PRO223 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue EDO C 504 |
Chain | Residue |
C | THR238 |
C | ASP244 |
C | ALA245 |
D | ARG91 |
site_id | AE6 |
Number of Residues | 5 |
Details | binding site for residue EDO C 505 |
Chain | Residue |
A | ASN251 |
C | PHE196 |
C | ASN197 |
C | LYS200 |
C | GLU227 |
site_id | AE7 |
Number of Residues | 7 |
Details | binding site for residue EDO C 506 |
Chain | Residue |
A | PHE196 |
A | ASN197 |
A | LYS200 |
A | GLU227 |
C | ASN251 |
C | ILE252 |
C | HOH658 |
site_id | AE8 |
Number of Residues | 9 |
Details | binding site for residue UXP D 501 |
Chain | Residue |
D | HIS117 |
D | GLY118 |
D | THR182 |
D | ASN183 |
D | CYS219 |
D | TYR239 |
D | HIS281 |
D | LEU284 |
D | ASN285 |
site_id | AE9 |
Number of Residues | 6 |
Details | binding site for residue EDO D 502 |
Chain | Residue |
C | HIS208 |
C | ARG234 |
D | PRO96 |
D | GLU99 |
D | HIS173 |
D | HOH643 |
site_id | AF1 |
Number of Residues | 3 |
Details | binding site for residue EDO D 503 |
Chain | Residue |
D | PRO270 |
D | ASP272 |
D | HOH631 |
site_id | AF2 |
Number of Residues | 4 |
Details | binding site for residue EDO D 504 |
Chain | Residue |
D | PRO266 |
D | ASP295 |
D | HOH615 |
D | HOH616 |
site_id | AF3 |
Number of Residues | 4 |
Details | binding site for residue EDO D 505 |
Chain | Residue |
D | SER124 |
D | ALA127 |
D | PHE139 |
D | PHE310 |
site_id | AF4 |
Number of Residues | 6 |
Details | binding site for residue DMS D 506 |
Chain | Residue |
D | ARG158 |
D | TYR159 |
D | GLU296 |
D | GLY297 |
D | ILE298 |
D | HOH603 |
site_id | AF5 |
Number of Residues | 8 |
Details | binding site for residue DMS D 507 |
Chain | Residue |
D | VAL220 |
D | ASP221 |
D | ASP222 |
D | PRO223 |
D | ARG226 |
G | VAL220 |
G | ASP221 |
G | PRO223 |
site_id | AF6 |
Number of Residues | 1 |
Details | binding site for residue CL D 508 |
Chain | Residue |
D | VAL94 |
site_id | AF7 |
Number of Residues | 8 |
Details | binding site for residue UXP E 501 |
Chain | Residue |
E | GLY118 |
E | THR182 |
E | ASN183 |
E | CYS219 |
E | TYR239 |
E | HIS281 |
E | LEU284 |
E | ASN285 |
site_id | AF8 |
Number of Residues | 2 |
Details | binding site for residue EDO E 502 |
Chain | Residue |
E | HOH633 |
F | ASP244 |
site_id | AF9 |
Number of Residues | 5 |
Details | binding site for residue EDO E 503 |
Chain | Residue |
E | ASN197 |
E | LYS200 |
E | GLU227 |
E | HOH604 |
F | ALA249 |
site_id | AG1 |
Number of Residues | 3 |
Details | binding site for residue EDO E 504 |
Chain | Residue |
E | PRO270 |
E | ASP272 |
E | HOH602 |
site_id | AG2 |
Number of Residues | 6 |
Details | binding site for residue EDO E 505 |
Chain | Residue |
B | LEU172 |
B | HIS173 |
B | ASN209 |
E | LEU172 |
E | GLU205 |
E | ASN209 |
site_id | AG3 |
Number of Residues | 2 |
Details | binding site for residue DMS E 506 |
Chain | Residue |
E | TYR159 |
E | GLU296 |
site_id | AG4 |
Number of Residues | 4 |
Details | binding site for residue DMS E 507 |
Chain | Residue |
E | ARG9 |
E | LEU31 |
E | GLY32 |
E | TYR33 |
site_id | AG5 |
Number of Residues | 1 |
Details | binding site for residue CL E 508 |
Chain | Residue |
E | VAL94 |
site_id | AG6 |
Number of Residues | 9 |
Details | binding site for residue UXP F 501 |
Chain | Residue |
F | HIS117 |
F | GLY118 |
F | THR182 |
F | ASN183 |
F | CYS219 |
F | TYR239 |
F | HIS281 |
F | LEU284 |
F | ASN285 |
site_id | AG7 |
Number of Residues | 4 |
Details | binding site for residue EDO F 502 |
Chain | Residue |
F | LEU229 |
F | THR238 |
F | ASP244 |
F | ALA245 |
site_id | AG8 |
Number of Residues | 5 |
Details | binding site for residue EDO F 503 |
Chain | Residue |
F | PRO96 |
F | GLU99 |
F | HIS173 |
H | HIS208 |
H | ARG234 |
site_id | AG9 |
Number of Residues | 3 |
Details | binding site for residue EDO F 504 |
Chain | Residue |
F | PRO270 |
F | LEU271 |
F | ASP272 |
site_id | AH1 |
Number of Residues | 5 |
Details | binding site for residue DMS F 505 |
Chain | Residue |
F | ARG158 |
F | TYR159 |
F | GLU296 |
F | HOH620 |
F | HOH638 |
site_id | AH2 |
Number of Residues | 1 |
Details | binding site for residue CL F 506 |
Chain | Residue |
F | VAL94 |
site_id | AH3 |
Number of Residues | 10 |
Details | binding site for residue UXP G 501 |
Chain | Residue |
G | HIS117 |
G | GLY118 |
G | THR182 |
G | ASN183 |
G | CYS219 |
G | TYR239 |
G | HIS281 |
G | LEU284 |
G | ASN285 |
G | HOH629 |
site_id | AH4 |
Number of Residues | 5 |
Details | binding site for residue EDO G 502 |
Chain | Residue |
A | HIS208 |
A | ARG234 |
G | PRO96 |
G | GLU99 |
G | HIS173 |
site_id | AH5 |
Number of Residues | 3 |
Details | binding site for residue EDO G 503 |
Chain | Residue |
G | PRO270 |
G | LEU271 |
G | ASP272 |
site_id | AH6 |
Number of Residues | 4 |
Details | binding site for residue DMS G 504 |
Chain | Residue |
F | HOH604 |
G | TYR159 |
G | GLU296 |
G | GLY297 |
site_id | AH7 |
Number of Residues | 1 |
Details | binding site for residue CL G 505 |
Chain | Residue |
G | VAL94 |
site_id | AH8 |
Number of Residues | 9 |
Details | binding site for residue UXP H 501 |
Chain | Residue |
H | HIS117 |
H | GLY118 |
H | THR182 |
H | ASN183 |
H | CYS219 |
H | TYR239 |
H | HIS281 |
H | LEU284 |
H | ASN285 |
site_id | AH9 |
Number of Residues | 5 |
Details | binding site for residue EDO H 502 |
Chain | Residue |
F | HIS208 |
F | ARG234 |
H | PRO96 |
H | GLU99 |
H | HIS173 |
site_id | AI1 |
Number of Residues | 5 |
Details | binding site for residue EDO H 503 |
Chain | Residue |
B | PRO223 |
H | ASP221 |
H | LEU241 |
H | LEU284 |
H | HOH603 |
site_id | AI2 |
Number of Residues | 3 |
Details | binding site for residue EDO H 504 |
Chain | Residue |
H | PRO270 |
H | ASP272 |
H | HOH630 |
site_id | AI3 |
Number of Residues | 4 |
Details | binding site for residue DMS H 505 |
Chain | Residue |
H | ARG158 |
H | TYR159 |
H | GLU296 |
H | HOH612 |
site_id | AI4 |
Number of Residues | 1 |
Details | binding site for residue CL H 506 |
Chain | Residue |
H | VAL94 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00046 |
Chain | Residue | Details |
A | GLY115 | |
B | GLY115 | |
C | GLY115 | |
D | GLY115 | |
E | GLY115 | |
F | GLY115 | |
G | GLY115 | |
H | GLY115 |