3V4T
E. cloacae C115D MURA liganded with UNAG
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008360 | biological_process | regulation of cell shape |
A | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
A | 0009252 | biological_process | peptidoglycan biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
A | 0051301 | biological_process | cell division |
A | 0071555 | biological_process | cell wall organization |
B | 0003824 | molecular_function | catalytic activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008360 | biological_process | regulation of cell shape |
B | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
B | 0009252 | biological_process | peptidoglycan biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
B | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
B | 0051301 | biological_process | cell division |
B | 0071555 | biological_process | cell wall organization |
C | 0003824 | molecular_function | catalytic activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0008360 | biological_process | regulation of cell shape |
C | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
C | 0009252 | biological_process | peptidoglycan biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
C | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
C | 0051301 | biological_process | cell division |
C | 0071555 | biological_process | cell wall organization |
D | 0003824 | molecular_function | catalytic activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0008360 | biological_process | regulation of cell shape |
D | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
D | 0009252 | biological_process | peptidoglycan biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
D | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
D | 0051301 | biological_process | cell division |
D | 0071555 | biological_process | cell wall organization |
E | 0003824 | molecular_function | catalytic activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0008360 | biological_process | regulation of cell shape |
E | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
E | 0009252 | biological_process | peptidoglycan biosynthetic process |
E | 0016740 | molecular_function | transferase activity |
E | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
E | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
E | 0051301 | biological_process | cell division |
E | 0071555 | biological_process | cell wall organization |
F | 0003824 | molecular_function | catalytic activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0008360 | biological_process | regulation of cell shape |
F | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
F | 0009252 | biological_process | peptidoglycan biosynthetic process |
F | 0016740 | molecular_function | transferase activity |
F | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
F | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
F | 0051301 | biological_process | cell division |
F | 0071555 | biological_process | cell wall organization |
G | 0003824 | molecular_function | catalytic activity |
G | 0005737 | cellular_component | cytoplasm |
G | 0008360 | biological_process | regulation of cell shape |
G | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
G | 0009252 | biological_process | peptidoglycan biosynthetic process |
G | 0016740 | molecular_function | transferase activity |
G | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
G | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
G | 0051301 | biological_process | cell division |
G | 0071555 | biological_process | cell wall organization |
H | 0003824 | molecular_function | catalytic activity |
H | 0005737 | cellular_component | cytoplasm |
H | 0008360 | biological_process | regulation of cell shape |
H | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
H | 0009252 | biological_process | peptidoglycan biosynthetic process |
H | 0016740 | molecular_function | transferase activity |
H | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
H | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
H | 0051301 | biological_process | cell division |
H | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE UD1 A 501 |
Chain | Residue |
A | ASN23 |
A | SER162 |
A | VAL163 |
A | GLY164 |
A | THR304 |
A | ASP305 |
A | ILE327 |
A | PHE328 |
A | EDO506 |
A | EDO507 |
A | HOH608 |
A | TRP95 |
A | HOH626 |
A | HOH653 |
A | ARG120 |
A | PRO121 |
A | VAL122 |
A | ASP123 |
A | LEU124 |
A | HIS125 |
A | LYS160 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT A 502 |
Chain | Residue |
A | TYR84 |
A | VAL87 |
A | SER110 |
A | LEU111 |
A | PRO112 |
A | GLY113 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 503 |
Chain | Residue |
A | ARG267 |
A | ILE273 |
A | GLU274 |
A | THR275 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 504 |
Chain | Residue |
A | ALA363 |
A | GLN364 |
A | THR386 |
A | VAL388 |
D | GLU140 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT A 505 |
Chain | Residue |
A | ASN350 |
C | GLU348 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | ARG91 |
A | HIS125 |
A | GLY164 |
A | UD1501 |
A | HOH653 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | VAL161 |
A | GLU188 |
A | PRO298 |
A | UD1501 |
A | HOH604 |
A | HOH663 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 508 |
Chain | Residue |
A | ASP260 |
A | LEU263 |
A | ARG267 |
B | HIS155 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 509 |
Chain | Residue |
A | ASP193 |
A | GLN255 |
site_id | BC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE UD1 B 501 |
Chain | Residue |
B | ASN23 |
B | TRP95 |
B | ARG120 |
B | PRO121 |
B | VAL122 |
B | ASP123 |
B | LEU124 |
B | HIS125 |
B | LYS160 |
B | SER162 |
B | VAL163 |
B | GLY164 |
B | THR304 |
B | ASP305 |
B | ILE327 |
B | PHE328 |
B | ACT502 |
B | EDO503 |
B | EDO504 |
B | HOH602 |
B | HOH608 |
B | HOH613 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT B 502 |
Chain | Residue |
B | THR326 |
B | ILE327 |
B | GLU329 |
B | UD1501 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 503 |
Chain | Residue |
B | TRP95 |
B | ARG120 |
B | HIS125 |
B | GLY164 |
B | UD1501 |
B | HOH602 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 504 |
Chain | Residue |
B | LYS22 |
B | LEU26 |
B | ASP49 |
B | MET90 |
B | ARG91 |
B | ALA92 |
B | ARG397 |
B | UD1501 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 505 |
Chain | Residue |
B | GLN255 |
B | HOH626 |
B | VAL192 |
B | ASP193 |
B | ASN196 |
B | TYR226 |
site_id | BC6 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE UD1 C 501 |
Chain | Residue |
C | ASN23 |
C | TRP95 |
C | ARG120 |
C | PRO121 |
C | VAL122 |
C | ASP123 |
C | LEU124 |
C | HIS125 |
C | SER162 |
C | VAL163 |
C | GLY164 |
C | THR304 |
C | ASP305 |
C | ILE327 |
C | PHE328 |
C | EDO504 |
C | HOH604 |
C | HOH605 |
C | HOH608 |
C | HOH616 |
C | HOH626 |
C | HOH629 |
C | HOH634 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT C 502 |
Chain | Residue |
C | ASP257 |
C | GLY276 |
C | GLU277 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT C 503 |
Chain | Residue |
C | LYS160 |
C | VAL161 |
C | ILE327 |
C | HOH615 |
C | HOH634 |
site_id | BC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 504 |
Chain | Residue |
C | ALA92 |
C | TRP95 |
C | ARG120 |
C | HIS125 |
C | GLY164 |
C | UD1501 |
C | HOH604 |
site_id | CC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO C 505 |
Chain | Residue |
C | THR52 |
C | LEU86 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 506 |
Chain | Residue |
C | VAL192 |
C | ASP193 |
C | ASN196 |
C | GLN255 |
site_id | CC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO C 507 |
Chain | Residue |
C | ARG252 |
C | ASN253 |
site_id | CC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE UD1 D 501 |
Chain | Residue |
D | ASN23 |
D | TRP95 |
D | ARG120 |
D | PRO121 |
D | VAL122 |
D | ASP123 |
D | LEU124 |
D | HIS125 |
D | LYS160 |
D | SER162 |
D | VAL163 |
D | GLY164 |
D | THR304 |
D | ASP305 |
D | ILE327 |
D | PHE328 |
D | EDO504 |
D | EDO506 |
D | EDO510 |
D | HOH602 |
D | HOH625 |
D | HOH659 |
site_id | CC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACT D 502 |
Chain | Residue |
D | ASN412 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT D 503 |
Chain | Residue |
D | GLN108 |
D | TYR142 |
D | LYS144 |
site_id | CC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 504 |
Chain | Residue |
D | ARG91 |
D | ALA92 |
D | TRP95 |
D | HIS125 |
D | GLY164 |
D | UD1501 |
D | EDO510 |
D | HOH602 |
site_id | CC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 505 |
Chain | Residue |
D | LYS22 |
D | LEU26 |
D | ASP49 |
D | ARG91 |
D | ALA92 |
D | LEU370 |
D | ARG397 |
D | EDO510 |
site_id | CC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 506 |
Chain | Residue |
D | VAL161 |
D | GLU188 |
D | PRO298 |
D | ILE327 |
D | UD1501 |
D | HOH624 |
site_id | DC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 507 |
Chain | Residue |
D | ILE244 |
D | GLU358 |
D | ILE382 |
H | ACT505 |
site_id | DC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 508 |
Chain | Residue |
D | ARG150 |
D | LEU175 |
D | GLU177 |
site_id | DC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO D 509 |
Chain | Residue |
A | ARG340 |
D | TYR84 |
D | VAL87 |
D | LYS88 |
D | SER110 |
D | LEU111 |
D | PRO112 |
D | GLY113 |
D | HOH637 |
site_id | DC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 510 |
Chain | Residue |
D | ARG120 |
D | LEU370 |
D | UD1501 |
D | EDO504 |
D | EDO505 |
site_id | DC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE UD1 E 501 |
Chain | Residue |
E | ASN23 |
E | TRP95 |
E | ARG120 |
E | PRO121 |
E | VAL122 |
E | ASP123 |
E | LEU124 |
E | HIS125 |
E | LYS160 |
E | SER162 |
E | VAL163 |
E | GLY164 |
E | THR304 |
E | ASP305 |
E | ILE327 |
E | PHE328 |
E | ACT502 |
E | EDO509 |
E | HOH603 |
E | HOH608 |
E | HOH618 |
E | HOH644 |
site_id | DC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT E 502 |
Chain | Residue |
E | LYS22 |
E | ARG120 |
E | LEU370 |
E | UD1501 |
site_id | DC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT E 503 |
Chain | Residue |
E | GLN7 |
E | PRO9 |
site_id | DC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE ACT E 504 |
Chain | Residue |
E | GLU65 |
site_id | DC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO E 505 |
Chain | Residue |
A | ASN412 |
E | ARG11 |
E | GLN13 |
site_id | EC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO E 506 |
Chain | Residue |
E | VAL316 |
E | GLU358 |
E | LYS359 |
E | LEU360 |
E | ILE382 |
site_id | EC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO E 507 |
Chain | Residue |
A | ARG11 |
A | SER245 |
E | HIS285 |
E | GLY286 |
E | LYS287 |
site_id | EC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO E 508 |
Chain | Residue |
E | ASP123 |
site_id | EC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO E 509 |
Chain | Residue |
E | ARG91 |
E | TRP95 |
E | ARG120 |
E | HIS125 |
E | GLY164 |
E | UD1501 |
E | HOH608 |
site_id | EC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO E 510 |
Chain | Residue |
E | ASP404 |
site_id | EC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO E 511 |
Chain | Residue |
E | PRO38 |
E | GLY224 |
H | GLU277 |
H | ASP278 |
site_id | EC7 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE UD1 F 501 |
Chain | Residue |
F | ASN23 |
F | TRP95 |
F | ARG120 |
F | PRO121 |
F | VAL122 |
F | ASP123 |
F | LEU124 |
F | HIS125 |
F | LYS160 |
F | SER162 |
F | VAL163 |
F | GLY164 |
F | THR304 |
F | ASP305 |
F | ILE327 |
F | PHE328 |
F | EDO505 |
F | HOH606 |
F | HOH612 |
F | HOH622 |
F | HOH625 |
F | HOH634 |
F | HOH635 |
site_id | EC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT F 503 |
Chain | Residue |
F | PHE328 |
F | GLU329 |
F | ARG331 |
F | PHE332 |
F | SER349 |
F | ASN350 |
site_id | EC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT F 504 |
Chain | Residue |
F | ARG288 |
F | GLU318 |
site_id | FC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO F 505 |
Chain | Residue |
F | ARG91 |
F | ILE94 |
F | TRP95 |
F | ARG120 |
F | HIS125 |
F | GLY164 |
F | UD1501 |
F | HOH606 |
site_id | FC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO F 506 |
Chain | Residue |
E | HIS155 |
F | ALA264 |
F | ARG267 |
site_id | FC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO F 507 |
Chain | Residue |
F | HOH644 |
site_id | FC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO F 508 |
Chain | Residue |
E | ARG295 |
F | LYS160 |
F | VAL161 |
F | ILE327 |
F | HOH656 |
site_id | FC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO F 509 |
Chain | Residue |
E | ALA261 |
E | ALA264 |
E | LYS265 |
E | GLU268 |
E | HOH636 |
F | VAL157 |
F | ASP159 |
site_id | FC6 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE UD1 G 501 |
Chain | Residue |
G | ASN23 |
G | TRP95 |
G | ARG120 |
G | PRO121 |
G | VAL122 |
G | ASP123 |
G | LEU124 |
G | LYS160 |
G | SER162 |
G | VAL163 |
G | GLY164 |
G | THR304 |
G | ASP305 |
G | ILE327 |
G | PHE328 |
G | ARG331 |
G | EDO502 |
G | HOH604 |
G | HOH614 |
G | HOH643 |
G | HOH646 |
G | HOH660 |
site_id | FC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO G 502 |
Chain | Residue |
G | ARG91 |
G | TRP95 |
G | HIS125 |
G | GLY164 |
G | UD1501 |
G | HOH643 |
site_id | FC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO G 503 |
Chain | Residue |
G | THR210 |
G | ASP211 |
H | GLY209 |
site_id | FC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO G 504 |
Chain | Residue |
G | LEU111 |
G | PRO121 |
G | VAL122 |
site_id | GC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO G 505 |
Chain | Residue |
G | ASN196 |
site_id | GC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO G 506 |
Chain | Residue |
G | ARG252 |
G | SER281 |
site_id | GC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO G 507 |
Chain | Residue |
G | ASP260 |
G | ALA264 |
G | ARG267 |
site_id | GC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO G 508 |
Chain | Residue |
G | GLN7 |
G | GLY8 |
G | PRO9 |
G | THR10 |
G | ASN412 |
site_id | GC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE UD1 H 501 |
Chain | Residue |
H | ASN23 |
H | TRP95 |
H | ARG120 |
H | PRO121 |
H | VAL122 |
H | ASP123 |
H | LEU124 |
H | LYS160 |
H | SER162 |
H | VAL163 |
H | GLY164 |
H | THR304 |
H | ASP305 |
H | ILE327 |
H | ACT503 |
H | HOH606 |
H | HOH607 |
site_id | GC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT H 502 |
Chain | Residue |
H | GLY207 |
H | GLN208 |
H | HOH639 |
site_id | GC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT H 503 |
Chain | Residue |
H | ARG91 |
H | TRP95 |
H | HIS125 |
H | GLY164 |
H | UD1501 |
H | HOH606 |
site_id | GC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT H 504 |
Chain | Residue |
H | LYS63 |
H | GLU65 |
H | TRP71 |
site_id | GC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT H 505 |
Chain | Residue |
D | THR10 |
D | ARG11 |
D | EDO507 |
H | HIS285 |
H | GLY286 |
H | LYS287 |
site_id | HC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT H 506 |
Chain | Residue |
H | PRO38 |
H | VAL225 |
site_id | HC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO H 507 |
Chain | Residue |
H | TYR84 |
H | VAL87 |
H | LYS88 |
H | SER110 |
H | LEU111 |
H | PRO112 |
H | GLY113 |
H | HOH655 |
site_id | HC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO H 508 |
Chain | Residue |
H | PRO27 |
H | ALA31 |
H | TRP95 |
H | PRO99 |
H | VAL167 |
H | THR168 |
H | SER171 |
H | HOH628 |
site_id | HC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO H 509 |
Chain | Residue |
H | ILE126 |
H | HOH644 |
site_id | HC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO H 510 |
Chain | Residue |
H | THR58 |
H | HOH610 |
site_id | HC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO H 511 |
Chain | Residue |
H | LYS88 |
H | THR89 |
H | ARG91 |
H | ASP115 |
H | ARG397 |
H | HOH641 |
H | HOH655 |
site_id | HC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO H 512 |
Chain | Residue |
H | SER19 |
H | GLY20 |
H | LYS22 |
H | PRO45 |
H | ASP231 |
H | GLU234 |
H | GLY398 |
H | TYR399 |
H | GLU400 |
H | HOH633 |
site_id | HC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO H 513 |
Chain | Residue |
H | PRO9 |
H | ASN412 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH |
Chain | Residue | Details |
A | ASP115 | |
B | ASP115 | |
C | ASP115 | |
D | ASP115 | |
E | ASP115 | |
F | ASP115 | |
G | ASP115 | |
H | ASP115 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | LYS22 | |
B | LYS22 | |
C | LYS22 | |
D | LYS22 | |
E | LYS22 | |
F | LYS22 | |
G | LYS22 | |
H | LYS22 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
Chain | Residue | Details |
A | ARG91 | |
B | ARG91 | |
C | ARG91 | |
D | ARG91 | |
E | ARG91 | |
F | ARG91 | |
G | ARG91 | |
H | ARG91 |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | ARG120 | |
D | ARG120 | |
D | ASP305 | |
D | ILE327 | |
E | ARG120 | |
E | ASP305 | |
E | ILE327 | |
F | ARG120 | |
F | ASP305 | |
F | ILE327 | |
G | ARG120 | |
A | ASP305 | |
G | ASP305 | |
G | ILE327 | |
H | ARG120 | |
H | ASP305 | |
H | ILE327 | |
A | ILE327 | |
B | ARG120 | |
B | ASP305 | |
B | ILE327 | |
C | ARG120 | |
C | ASP305 | |
C | ILE327 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | LYS160 | |
B | LYS160 | |
C | LYS160 | |
D | LYS160 | |
E | LYS160 | |
F | LYS160 | |
G | LYS160 | |
H | LYS160 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791 |
Chain | Residue | Details |
A | ASP115 | |
B | ASP115 | |
C | ASP115 | |
D | ASP115 | |
E | ASP115 | |
F | ASP115 | |
G | ASP115 | |
H | ASP115 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 369 |
Chain | Residue | Details |
A | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
A | ASN23 | electrostatic stabiliser, hydrogen bond donor |
A | ASP115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
A | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
A | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 369 |
Chain | Residue | Details |
B | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
B | ASN23 | electrostatic stabiliser, hydrogen bond donor |
B | ASP115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
B | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
B | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 369 |
Chain | Residue | Details |
C | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
C | ASN23 | electrostatic stabiliser, hydrogen bond donor |
C | ASP115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
C | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
C | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 369 |
Chain | Residue | Details |
D | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
D | ASN23 | electrostatic stabiliser, hydrogen bond donor |
D | ASP115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
D | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
D | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA5 |
Number of Residues | 6 |
Details | M-CSA 369 |
Chain | Residue | Details |
E | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
E | ASN23 | electrostatic stabiliser, hydrogen bond donor |
E | ASP115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
E | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
E | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
E | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA6 |
Number of Residues | 6 |
Details | M-CSA 369 |
Chain | Residue | Details |
F | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
F | ASN23 | electrostatic stabiliser, hydrogen bond donor |
F | ASP115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
F | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
F | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
F | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA7 |
Number of Residues | 6 |
Details | M-CSA 369 |
Chain | Residue | Details |
G | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
G | ASN23 | electrostatic stabiliser, hydrogen bond donor |
G | ASP115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
G | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
G | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
G | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA8 |
Number of Residues | 6 |
Details | M-CSA 369 |
Chain | Residue | Details |
H | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
H | ASN23 | electrostatic stabiliser, hydrogen bond donor |
H | ASP115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
H | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
H | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
H | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |