3V5V
UNLIGANDED E.CLOACAE C115D MURA
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PEG A 501 |
Chain | Residue |
A | ARG232 |
A | PRO303 |
A | HOH650 |
A | HOH654 |
A | ASP257 |
A | THR258 |
A | LEU259 |
A | ASP260 |
A | ALA261 |
A | VAL262 |
A | HIS299 |
A | PRO300 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PEG A 502 |
Chain | Residue |
A | ASP260 |
A | ALA261 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | GLU183 |
A | ASN184 |
A | ASP211 |
B | LYS265 |
B | THR293 |
B | ARG295 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | VAL101 |
A | ALA102 |
A | ARG103 |
A | GLY149 |
A | ARG150 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | ASP51 |
A | LYS55 |
A | THR58 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | PRO27 |
A | PHE30 |
A | ALA31 |
A | TRP95 |
A | PRO99 |
A | VAL167 |
A | THR168 |
A | SER171 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 508 |
Chain | Residue |
A | GLU188 |
A | ALA297 |
A | PHE302 |
A | PRO303 |
A | THR304 |
A | ILE327 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 509 |
Chain | Residue |
A | PRO230 |
A | ASP231 |
A | ARG232 |
A | THR235 |
A | ALA254 |
A | GLN255 |
A | THR258 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 510 |
Chain | Residue |
A | GLU15 |
A | GLU177 |
A | ALA408 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 511 |
Chain | Residue |
A | ASN79 |
A | PHE80 |
A | SER81 |
A | GLN106 |
A | HOH703 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PGE B 501 |
Chain | Residue |
B | ASN23 |
B | ALA92 |
B | ILE94 |
B | TRP95 |
B | VAL163 |
B | GLU190 |
B | HOH718 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 502 |
Chain | Residue |
A | ASP85 |
B | GLU40 |
B | GLN42 |
site_id | BC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 503 |
Chain | Residue |
B | ARG252 |
B | TRP279 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 504 |
Chain | Residue |
B | GLU15 |
B | VAL16 |
B | THR17 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 505 |
Chain | Residue |
A | HIS155 |
A | VAL157 |
A | GLU183 |
A | ARG212 |
B | ALA291 |
B | VAL292 |
B | THR293 |
B | THR320 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 506 |
Chain | Residue |
B | ALA154 |
B | HIS155 |
B | THR179 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 507 |
Chain | Residue |
B | GLU188 |
B | ARG232 |
B | PRO303 |
B | THR304 |
B | ASP305 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 508 |
Chain | Residue |
B | PRO230 |
B | ARG232 |
B | THR235 |
B | ALA254 |
B | GLN255 |
B | THR258 |
site_id | CC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PEG C 501 |
Chain | Residue |
C | HIS299 |
C | PRO300 |
C | PRO303 |
C | HOH661 |
C | ASP257 |
C | LEU259 |
C | ASP260 |
C | ALA261 |
C | VAL262 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 502 |
Chain | Residue |
A | GLU139 |
C | GLU135 |
C | ILE136 |
C | LYS137 |
C | LYS144 |
C | SER146 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 503 |
Chain | Residue |
C | ARG295 |
C | ALA301 |
C | PHE302 |
C | EDO504 |
D | ARG187 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 504 |
Chain | Residue |
C | ASP260 |
C | ALA261 |
C | ALA264 |
C | EDO503 |
C | HOH690 |
D | ARG187 |
site_id | CC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO C 505 |
Chain | Residue |
C | TRP95 |
C | HOH698 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 506 |
Chain | Residue |
C | ASP49 |
C | THR89 |
C | MET90 |
site_id | CC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 507 |
Chain | Residue |
C | LYS204 |
C | SER206 |
C | THR214 |
C | GLU216 |
site_id | CC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 508 |
Chain | Residue |
A | LEU138 |
A | GLY141 |
C | GLU130 |
C | GLY133 |
C | ALA134 |
site_id | CC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 509 |
Chain | Residue |
C | GLN7 |
C | PRO9 |
C | THR10 |
C | ASN412 |
C | HOH677 |
D | ARG252 |
site_id | DC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT C 510 |
Chain | Residue |
C | ARG187 |
C | THR210 |
C | ASP211 |
C | HOH683 |
D | LYS265 |
D | GLU268 |
site_id | DC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PEG D 501 |
Chain | Residue |
D | ASP260 |
D | ALA261 |
D | PRO300 |
D | HOH692 |
site_id | DC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 502 |
Chain | Residue |
D | ALA21 |
D | LYS22 |
D | ASN23 |
D | GLU190 |
D | ASP231 |
site_id | DC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO D 503 |
Chain | Residue |
D | LYS55 |
site_id | DC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 504 |
Chain | Residue |
D | GLU15 |
D | VAL16 |
D | LYS405 |
D | ALA408 |
site_id | DC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO D 505 |
Chain | Residue |
D | PRO27 |
D | PHE30 |
D | ALA31 |
D | TRP95 |
D | PRO99 |
D | VAL167 |
D | SER171 |
site_id | DC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO D 506 |
Chain | Residue |
D | SER206 |
D | GLY207 |
D | ARG212 |
D | THR214 |
site_id | DC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 507 |
Chain | Residue |
D | ASN43 |
D | ARG227 |
D | VAL228 |
D | LEU229 |
D | PRO230 |
D | ASN253 |
site_id | DC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 508 |
Chain | Residue |
D | GLU188 |
D | ALA297 |
D | THR304 |
D | HOH629 |
D | HOH709 |
site_id | EC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO D 509 |
Chain | Residue |
D | GLU15 |
D | ALA408 |
site_id | EC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO D 510 |
Chain | Residue |
D | SER245 |
site_id | EC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 511 |
Chain | Residue |
D | LEU229 |
D | PRO230 |
D | ASP231 |
D | ARG232 |
D | THR235 |
D | ALA254 |
D | GLN255 |
D | THR258 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
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 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
B | LYS22 | |
C | LYS22 | |
A | LYS22 | |
D | LYS22 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
Chain | Residue | Details |
A | ARG91 | |
B | ARG91 | |
C | ARG91 | |
D | ARG91 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
B | ASP305 | |
B | ILE327 | |
C | ARG120 | |
C | ASP305 | |
C | ILE327 | |
D | ARG120 | |
D | ASP305 | |
D | ILE327 | |
A | ARG120 | |
A | ASP305 | |
A | ILE327 | |
B | ARG120 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | LYS160 | |
B | LYS160 | |
C | LYS160 | |
D | LYS160 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
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 |
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 |