1T36
Crystal structure of E. coli carbamoyl phosphate synthetase small subunit mutant C248D complexed with uridine 5'-monophosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004087 | molecular_function | carbamoyl-phosphate synthase (ammonia) activity |
| A | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005951 | cellular_component | carbamoyl-phosphate synthase complex |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016874 | molecular_function | ligase activity |
| A | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| A | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005951 | cellular_component | carbamoyl-phosphate synthase complex |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004087 | molecular_function | carbamoyl-phosphate synthase (ammonia) activity |
| C | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005951 | cellular_component | carbamoyl-phosphate synthase complex |
| C | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| C | 0006526 | biological_process | L-arginine biosynthetic process |
| C | 0006541 | biological_process | glutamine metabolic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016597 | molecular_function | amino acid binding |
| C | 0016874 | molecular_function | ligase activity |
| C | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| C | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| C | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| D | 0004359 | molecular_function | glutaminase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005951 | cellular_component | carbamoyl-phosphate synthase complex |
| D | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| D | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| D | 0006526 | biological_process | L-arginine biosynthetic process |
| D | 0006541 | biological_process | glutamine metabolic process |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016874 | molecular_function | ligase activity |
| D | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| D | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| D | 0046982 | molecular_function | protein heterodimerization activity |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004087 | molecular_function | carbamoyl-phosphate synthase (ammonia) activity |
| E | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0005951 | cellular_component | carbamoyl-phosphate synthase complex |
| E | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| E | 0006526 | biological_process | L-arginine biosynthetic process |
| E | 0006541 | biological_process | glutamine metabolic process |
| E | 0008652 | biological_process | amino acid biosynthetic process |
| E | 0016597 | molecular_function | amino acid binding |
| E | 0016874 | molecular_function | ligase activity |
| E | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| E | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| E | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| F | 0004359 | molecular_function | glutaminase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0005951 | cellular_component | carbamoyl-phosphate synthase complex |
| F | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| F | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| F | 0006526 | biological_process | L-arginine biosynthetic process |
| F | 0006541 | biological_process | glutamine metabolic process |
| F | 0008652 | biological_process | amino acid biosynthetic process |
| F | 0016874 | molecular_function | ligase activity |
| F | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| F | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| F | 0046982 | molecular_function | protein heterodimerization activity |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0004087 | molecular_function | carbamoyl-phosphate synthase (ammonia) activity |
| G | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0005951 | cellular_component | carbamoyl-phosphate synthase complex |
| G | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| G | 0006526 | biological_process | L-arginine biosynthetic process |
| G | 0006541 | biological_process | glutamine metabolic process |
| G | 0008652 | biological_process | amino acid biosynthetic process |
| G | 0016597 | molecular_function | amino acid binding |
| G | 0016874 | molecular_function | ligase activity |
| G | 0016879 | molecular_function | ligase activity, forming carbon-nitrogen bonds |
| G | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| G | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0004088 | molecular_function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity |
| H | 0004359 | molecular_function | glutaminase activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0005951 | cellular_component | carbamoyl-phosphate synthase complex |
| H | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| H | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| H | 0006526 | biological_process | L-arginine biosynthetic process |
| H | 0006541 | biological_process | glutamine metabolic process |
| H | 0008652 | biological_process | amino acid biosynthetic process |
| H | 0016874 | molecular_function | ligase activity |
| H | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| H | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| H | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 1074 |
| Chain | Residue |
| A | GLU299 |
| A | ASN301 |
| A | PO41078 |
| A | ADP1087 |
| A | HOH1191 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 1075 |
| Chain | Residue |
| A | HOH1605 |
| A | GLN285 |
| A | GLU299 |
| A | PO41078 |
| A | ADP1087 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 1076 |
| Chain | Residue |
| A | GLU215 |
| A | ASN236 |
| A | ASP238 |
| A | ALA239 |
| A | ILE242 |
| A | SER247 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K A 1077 |
| Chain | Residue |
| A | ALA126 |
| A | GLU127 |
| A | GLU299 |
| A | MET300 |
| A | ASN301 |
| A | HOH1193 |
| A | HOH1607 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1078 |
| Chain | Residue |
| A | MET174 |
| A | GLY175 |
| A | HIS243 |
| A | GLN285 |
| A | GLU299 |
| A | ASN301 |
| A | ARG303 |
| A | ARG306 |
| A | MN1074 |
| A | MN1075 |
| A | ADP1087 |
| A | HOH1130 |
| A | HOH1305 |
| A | HOH1306 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 1079 |
| Chain | Residue |
| A | GLN829 |
| A | GLU841 |
| A | ADP1088 |
| A | HOH1608 |
| A | HOH1903 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 1080 |
| Chain | Residue |
| A | GLU761 |
| A | HIS781 |
| A | GLU783 |
| A | GLN784 |
| A | VAL787 |
| A | SER792 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1081 |
| Chain | Residue |
| A | GLN93 |
| A | MET174 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 1082 |
| Chain | Residue |
| A | THR143 |
| A | ALA144 |
| A | HOH1202 |
| A | HOH1203 |
| A | HOH1204 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 1083 |
| Chain | Residue |
| A | TRP71 |
| A | HOH1622 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1084 |
| Chain | Residue |
| A | ASN289 |
| A | ASN292 |
| A | ARG294 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 1085 |
| Chain | Residue |
| A | ALA370 |
| A | ASN371 |
| A | PHE900 |
| A | PRO901 |
| A | GLY902 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1086 |
| Chain | Residue |
| A | LYS475 |
| A | ASN485 |
| A | PHE488 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 383 |
| Chain | Residue |
| A | HOH1456 |
| A | HOH1457 |
| B | HIS16 |
| B | ASP112 |
| B | HOH3394 |
| B | HOH3605 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 1074 |
| Chain | Residue |
| C | GLU299 |
| C | ASN301 |
| C | MN1075 |
| C | PO41078 |
| C | ADP1089 |
| C | HOH1191 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN C 1075 |
| Chain | Residue |
| C | GLN285 |
| C | GLU299 |
| C | MN1074 |
| C | PO41078 |
| C | ADP1089 |
| C | HOH1587 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 1076 |
| Chain | Residue |
| C | GLU215 |
| C | ASN236 |
| C | ASP238 |
| C | ALA239 |
| C | ILE242 |
| C | SER247 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 1077 |
| Chain | Residue |
| C | ALA126 |
| C | GLU127 |
| C | GLU299 |
| C | MET300 |
| C | ASN301 |
| C | HOH1193 |
| site_id | CC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PO4 C 1078 |
| Chain | Residue |
| C | GLY175 |
| C | HIS243 |
| C | GLN285 |
| C | GLU299 |
| C | ASN301 |
| C | ARG303 |
| C | ARG306 |
| C | MN1074 |
| C | MN1075 |
| C | ADP1089 |
| C | HOH1191 |
| C | HOH1301 |
| C | MET174 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 1079 |
| Chain | Residue |
| C | GLN829 |
| C | GLU841 |
| C | ADP1090 |
| C | HOH1589 |
| C | HOH1590 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 1080 |
| Chain | Residue |
| C | GLU761 |
| C | HIS781 |
| C | GLU783 |
| C | GLN784 |
| C | VAL787 |
| C | SER792 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 1081 |
| Chain | Residue |
| C | THR173 |
| C | MET174 |
| C | HOH1127 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K C 1082 |
| Chain | Residue |
| C | THR143 |
| C | ALA144 |
| C | HOH1201 |
| C | HOH1202 |
| site_id | CC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL C 1083 |
| Chain | Residue |
| C | TRP71 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 1084 |
| Chain | Residue |
| C | ASN289 |
| C | ASN292 |
| C | ARG294 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 1085 |
| Chain | Residue |
| C | ALA370 |
| C | ASN371 |
| C | PHE900 |
| C | PRO901 |
| C | GLY902 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 1086 |
| Chain | Residue |
| C | LYS475 |
| C | ASN485 |
| C | HOH1607 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 383 |
| Chain | Residue |
| C | HOH1451 |
| D | HIS16 |
| D | ASP112 |
| D | HOH2331 |
| D | HOH2536 |
| site_id | DC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 384 |
| Chain | Residue |
| C | GLU549 |
| D | PHE15 |
| D | ASP114 |
| D | HOH2330 |
| site_id | DC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 1087 |
| Chain | Residue |
| C | PHE578 |
| C | ARG845 |
| C | ALA847 |
| C | ARG848 |
| site_id | DC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 C 1088 |
| Chain | Residue |
| C | GLU560 |
| C | ASP592 |
| site_id | DC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN E 1074 |
| Chain | Residue |
| E | GLU299 |
| E | ASN301 |
| E | PO41078 |
| E | ADP1089 |
| E | HOH1193 |
| site_id | DC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN E 1075 |
| Chain | Residue |
| E | GLN285 |
| E | GLU299 |
| E | PO41078 |
| E | ADP1089 |
| E | HOH1597 |
| site_id | DC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K E 1076 |
| Chain | Residue |
| E | GLU215 |
| E | ASN236 |
| E | ASP238 |
| E | ALA239 |
| E | ILE242 |
| E | SER247 |
| site_id | DC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K E 1077 |
| Chain | Residue |
| E | ALA126 |
| E | GLU127 |
| E | GLU299 |
| E | MET300 |
| E | ASN301 |
| E | HOH1193 |
| E | HOH1195 |
| site_id | DC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PO4 E 1078 |
| Chain | Residue |
| E | MET174 |
| E | GLY175 |
| E | HIS243 |
| E | GLN285 |
| E | GLU299 |
| E | ASN301 |
| E | ARG303 |
| E | ARG306 |
| E | MN1074 |
| E | MN1075 |
| E | ADP1089 |
| E | HOH1129 |
| E | HOH1303 |
| site_id | EC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN E 1079 |
| Chain | Residue |
| E | GLN829 |
| E | GLU841 |
| E | ADP1090 |
| E | HOH1601 |
| E | HOH1602 |
| site_id | EC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K E 1080 |
| Chain | Residue |
| E | GLU761 |
| E | HIS781 |
| E | GLU783 |
| E | GLN784 |
| E | VAL787 |
| E | SER792 |
| site_id | EC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K E 1081 |
| Chain | Residue |
| E | ASP84 |
| E | GLY112 |
| E | THR114 |
| E | HOH1095 |
| E | HOH1605 |
| site_id | EC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL E 1082 |
| Chain | Residue |
| E | THR173 |
| E | MET174 |
| site_id | EC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K E 1083 |
| Chain | Residue |
| E | THR143 |
| E | ALA144 |
| E | HOH1202 |
| E | HOH1203 |
| site_id | EC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL E 1084 |
| Chain | Residue |
| E | TRP71 |
| site_id | EC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL E 1085 |
| Chain | Residue |
| E | ASN289 |
| E | ASN292 |
| E | ARG294 |
| site_id | EC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL E 1086 |
| Chain | Residue |
| E | ALA370 |
| E | ASN371 |
| E | PHE900 |
| E | PRO901 |
| E | GLY902 |
| site_id | EC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL E 1087 |
| Chain | Residue |
| E | LYS475 |
| E | ASN485 |
| E | HOH1614 |
| site_id | FC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K F 383 |
| Chain | Residue |
| E | HOH1447 |
| F | HIS16 |
| F | ASP112 |
| F | HOH1308 |
| site_id | FC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL F 384 |
| Chain | Residue |
| E | GLU549 |
| E | HOH1447 |
| F | PHE15 |
| F | ASP114 |
| F | HOH1307 |
| site_id | FC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL E 1088 |
| Chain | Residue |
| E | ALA847 |
| E | ARG848 |
| site_id | FC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MN G 1074 |
| Chain | Residue |
| G | MET174 |
| G | GLU299 |
| G | ASN301 |
| G | MN1075 |
| G | PO41078 |
| G | ADP1089 |
| G | HOH1190 |
| site_id | FC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN G 1075 |
| Chain | Residue |
| G | GLN285 |
| G | GLU299 |
| G | MN1074 |
| G | PO41078 |
| G | ADP1089 |
| G | HOH1549 |
| site_id | FC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K G 1076 |
| Chain | Residue |
| G | GLU215 |
| G | ASN236 |
| G | ASP238 |
| G | ALA239 |
| G | ILE242 |
| G | SER247 |
| site_id | FC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K G 1077 |
| Chain | Residue |
| G | ALA126 |
| G | GLU127 |
| G | GLU299 |
| G | MET300 |
| G | ASN301 |
| G | HOH1190 |
| G | HOH1191 |
| site_id | FC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PO4 G 1078 |
| Chain | Residue |
| G | MET174 |
| G | GLY175 |
| G | HIS243 |
| G | GLN285 |
| G | GLU299 |
| G | ASN301 |
| G | ARG303 |
| G | ARG306 |
| G | MN1074 |
| G | MN1075 |
| G | ADP1089 |
| G | HOH1130 |
| G | HOH1289 |
| G | HOH1549 |
| site_id | FC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN G 1079 |
| Chain | Residue |
| G | GLN829 |
| G | GLU841 |
| G | ADP1090 |
| G | HOH1550 |
| G | HOH1551 |
| site_id | GC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K G 1080 |
| Chain | Residue |
| G | GLU761 |
| G | HIS781 |
| G | GLU783 |
| G | GLN784 |
| G | VAL787 |
| G | SER792 |
| site_id | GC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K G 1081 |
| Chain | Residue |
| G | ASP84 |
| G | GLY112 |
| G | THR114 |
| site_id | GC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL G 1082 |
| Chain | Residue |
| G | GLN93 |
| G | THR173 |
| G | MET174 |
| G | NET1092 |
| G | HOH1122 |
| site_id | GC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K G 1083 |
| Chain | Residue |
| G | THR143 |
| G | ALA144 |
| G | HOH1198 |
| G | HOH1199 |
| site_id | GC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL G 1084 |
| Chain | Residue |
| G | TRP71 |
| site_id | GC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL G 1085 |
| Chain | Residue |
| G | ASN289 |
| G | ASN292 |
| G | ARG294 |
| site_id | GC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL G 1086 |
| Chain | Residue |
| G | ASN371 |
| G | PHE900 |
| G | PRO901 |
| G | GLY902 |
| G | HOH1246 |
| site_id | GC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL G 1087 |
| Chain | Residue |
| G | LYS475 |
| G | ASN485 |
| G | PHE488 |
| G | HOH1419 |
| site_id | GC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K H 383 |
| Chain | Residue |
| G | HOH1422 |
| G | HOH1423 |
| H | HIS16 |
| H | ASP112 |
| site_id | HC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL H 384 |
| Chain | Residue |
| H | PHE15 |
| H | ASP114 |
| site_id | HC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL G 1088 |
| Chain | Residue |
| G | ARG845 |
| G | ALA847 |
| G | ARG848 |
| site_id | HC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL H 385 |
| Chain | Residue |
| H | TRP170 |
| H | THR171 |
| H | GLN172 |
| site_id | HC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ADP A 1087 |
| Chain | Residue |
| A | ARG129 |
| A | ILE167 |
| A | ARG169 |
| A | THR173 |
| A | MET174 |
| A | GLY175 |
| A | GLY176 |
| A | ASP207 |
| A | GLU208 |
| A | LEU210 |
| A | ILE211 |
| A | GLU215 |
| A | MET240 |
| A | GLY241 |
| A | ILE242 |
| A | HIS243 |
| A | THR244 |
| A | GLN285 |
| A | ILE298 |
| A | GLU299 |
| A | THR376 |
| A | MN1074 |
| A | MN1075 |
| A | PO41078 |
| A | HOH1191 |
| A | HOH1231 |
| A | HOH1244 |
| A | HOH1605 |
| site_id | HC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP A 1088 |
| Chain | Residue |
| A | PRO690 |
| A | ARG715 |
| A | MET725 |
| A | HIS754 |
| A | PHE755 |
| A | LEU756 |
| A | GLU761 |
| A | ALA785 |
| A | GLY786 |
| A | VAL787 |
| A | HIS788 |
| A | SER789 |
| A | GLN829 |
| A | GLU841 |
| A | PRO909 |
| A | MN1079 |
| A | HOH1499 |
| A | HOH1522 |
| A | HOH1526 |
| A | HOH1608 |
| A | HOH1609 |
| A | HOH1903 |
| site_id | HC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ORN A 1089 |
| Chain | Residue |
| A | GLU783 |
| A | ASP791 |
| A | ALA793 |
| A | GLU892 |
| A | LEU907 |
| A | TYR1040 |
| A | ASP1041 |
| A | THR1042 |
| A | HOH1538 |
| A | HOH1564 |
| site_id | HC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NET A 1090 |
| Chain | Residue |
| A | THR94 |
| A | ASN97 |
| A | ASN936 |
| site_id | HC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE U5P A 1091 |
| Chain | Residue |
| A | SER948 |
| A | VAL949 |
| A | LYS954 |
| A | THR974 |
| A | GLY976 |
| A | THR977 |
| A | LYS993 |
| A | ASN1015 |
| A | THR1016 |
| A | THR1017 |
| A | ASP1025 |
| A | SER1026 |
| A | ILE1029 |
| A | HOH1590 |
| site_id | HC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ADP C 1089 |
| Chain | Residue |
| C | ARG129 |
| C | ILE167 |
| C | ARG169 |
| C | THR173 |
| C | MET174 |
| C | GLY175 |
| C | GLY176 |
| C | GLU208 |
| C | SER209 |
| C | LEU210 |
| C | ILE211 |
| C | GLU215 |
| C | MET240 |
| C | GLY241 |
| C | ILE242 |
| C | HIS243 |
| C | THR244 |
| C | GLN285 |
| C | ILE298 |
| C | GLU299 |
| C | THR376 |
| C | MN1074 |
| C | MN1075 |
| C | PO41078 |
| C | HOH1191 |
| C | HOH1229 |
| C | HOH1244 |
| C | HOH1587 |
| site_id | IC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ADP C 1090 |
| Chain | Residue |
| C | ARG715 |
| C | MET725 |
| C | HIS754 |
| C | PHE755 |
| C | LEU756 |
| C | GLU761 |
| C | ALA785 |
| C | GLY786 |
| C | VAL787 |
| C | HIS788 |
| C | SER789 |
| C | GLN829 |
| C | GLU841 |
| C | MN1079 |
| C | HOH1515 |
| C | HOH1516 |
| C | HOH1589 |
| C | HOH1590 |
| site_id | IC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ORN C 1091 |
| Chain | Residue |
| C | GLU783 |
| C | ASP791 |
| C | GLU892 |
| C | LEU907 |
| C | TYR1040 |
| C | ASP1041 |
| C | THR1042 |
| C | HOH1530 |
| C | HOH1548 |
| site_id | IC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NET C 1092 |
| Chain | Residue |
| C | THR94 |
| C | ASN97 |
| site_id | IC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE U5P C 1093 |
| Chain | Residue |
| C | SER948 |
| C | VAL949 |
| C | LYS954 |
| C | THR974 |
| C | GLY976 |
| C | THR977 |
| C | LYS993 |
| C | ASN1015 |
| C | THR1016 |
| C | THR1017 |
| C | ALA1022 |
| C | SER1026 |
| C | ILE1029 |
| C | HOH1576 |
| C | HOH1846 |
| site_id | IC5 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP E 1089 |
| Chain | Residue |
| E | ARG129 |
| E | ILE167 |
| E | ARG169 |
| E | MET174 |
| E | GLY175 |
| E | GLY176 |
| E | GLU208 |
| E | LEU210 |
| E | ILE211 |
| E | GLU215 |
| E | MET240 |
| E | GLY241 |
| E | ILE242 |
| E | HIS243 |
| E | THR244 |
| E | GLN285 |
| E | ILE298 |
| E | GLU299 |
| E | THR376 |
| E | MN1074 |
| E | MN1075 |
| E | PO41078 |
| E | HOH1193 |
| E | HOH1227 |
| E | HOH1244 |
| E | HOH1597 |
| site_id | IC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP E 1090 |
| Chain | Residue |
| E | PRO690 |
| E | ARG715 |
| E | MET725 |
| E | HIS754 |
| E | PHE755 |
| E | LEU756 |
| E | GLU761 |
| E | ALA785 |
| E | GLY786 |
| E | VAL787 |
| E | HIS788 |
| E | SER789 |
| E | GLN829 |
| E | GLU841 |
| E | MN1079 |
| E | HOH1520 |
| E | HOH1521 |
| E | HOH1525 |
| E | HOH1598 |
| E | HOH1599 |
| E | HOH1600 |
| E | HOH1602 |
| site_id | IC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ORN E 1091 |
| Chain | Residue |
| E | GLU783 |
| E | ASP791 |
| E | GLU892 |
| E | LEU907 |
| E | TYR1040 |
| E | ASP1041 |
| E | THR1042 |
| E | HOH1537 |
| E | HOH1560 |
| E | HOH1570 |
| site_id | IC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NET E 1092 |
| Chain | Residue |
| E | GLN22 |
| E | GLN93 |
| E | THR94 |
| site_id | IC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE U5P E 1093 |
| Chain | Residue |
| E | SER948 |
| E | VAL949 |
| E | ARG950 |
| E | LYS954 |
| E | THR974 |
| E | GLY976 |
| E | THR977 |
| E | LYS993 |
| E | ASN1015 |
| E | THR1016 |
| E | THR1017 |
| E | ASP1025 |
| E | SER1026 |
| E | ILE1029 |
| E | HOH1585 |
| E | HOH1839 |
| E | HOH1847 |
| site_id | JC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ADP G 1089 |
| Chain | Residue |
| G | ARG129 |
| G | ILE167 |
| G | ARG169 |
| G | THR173 |
| G | MET174 |
| G | GLY175 |
| G | GLY176 |
| G | GLU208 |
| G | LEU210 |
| G | ILE211 |
| G | GLU215 |
| G | MET240 |
| G | GLY241 |
| G | ILE242 |
| G | HIS243 |
| G | THR244 |
| G | GLN285 |
| G | ILE298 |
| G | GLU299 |
| G | THR376 |
| G | MN1074 |
| G | MN1075 |
| G | PO41078 |
| G | HOH1222 |
| G | HOH1237 |
| G | HOH1548 |
| G | HOH1549 |
| site_id | JC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP G 1090 |
| Chain | Residue |
| G | ARG715 |
| G | HIS754 |
| G | PHE755 |
| G | LEU756 |
| G | GLU761 |
| G | ALA785 |
| G | GLY786 |
| G | VAL787 |
| G | HIS788 |
| G | SER789 |
| G | GLN829 |
| G | GLU841 |
| G | MN1079 |
| G | HOH1474 |
| G | HOH1478 |
| G | HOH1550 |
| G | HOH1551 |
| site_id | JC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ORN G 1091 |
| Chain | Residue |
| G | GLU783 |
| G | ASP791 |
| G | GLU892 |
| G | LEU907 |
| G | TYR1040 |
| G | ASP1041 |
| G | THR1042 |
| G | HOH1488 |
| G | HOH1511 |
| G | HOH1554 |
| site_id | JC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NET G 1092 |
| Chain | Residue |
| G | GLN22 |
| G | THR94 |
| G | ASN97 |
| G | CL1082 |
| site_id | JC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE U5P G 1093 |
| Chain | Residue |
| G | SER948 |
| G | VAL949 |
| G | LYS954 |
| G | THR974 |
| G | GLY976 |
| G | THR977 |
| G | LYS993 |
| G | ASN1015 |
| G | THR1016 |
| G | THR1017 |
| G | ALA1022 |
| G | ASP1025 |
| G | SER1026 |
| G | ILE1029 |
| G | HOH1537 |
Functional Information from PROSITE/UniProt
| site_id | PS00866 |
| Number of Residues | 15 |
| Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. FPCIIRPSftmGGsG |
| Chain | Residue | Details |
| A | PHE164-GLY178 | |
| A | TYR710-ALA724 |
| site_id | PS00867 |
| Number of Residues | 8 |
| Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. VIEMNPRV |
| Chain | Residue | Details |
| A | VAL297-VAL304 | |
| A | LEU839-ALA846 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 780 |
| Details | Domain: {"description":"ATP-grasp 1","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 544 |
| Details | Domain: {"description":"MGS-like","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1604 |
| Details | Region: {"description":"Carboxyphosphate synthetic domain","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 596 |
| Details | Region: {"description":"Oligomerization domain","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 544 |
| Details | Region: {"description":"Allosteric domain","evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10029528","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A9X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1C30","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1C3O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1CS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JDB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M6V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T36","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428826","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10029528","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10089390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10428826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10587438","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9636022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10428826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9636022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10029528","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10089390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10428826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9636022","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CE8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10029528","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10089390","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 748 |
| Details | Domain: {"description":"Glutamine amidotransferase type-1","evidences":[{"source":"HAMAP-Rule","id":"MF_01209","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01209","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01209","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01209","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10587438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1C3O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| F | HIS353 | |
| F | CYS269 | |
| F | GLU355 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| H | HIS353 | |
| H | CYS269 | |
| H | GLU355 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | HIS353 | |
| B | CYS269 | |
| B | GLU355 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| D | HIS353 | |
| D | CYS269 | |
| D | GLU355 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| B | HIS353 | |
| B | CYS269 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| D | HIS353 | |
| D | CYS269 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| F | HIS353 | |
| F | CYS269 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bxr |
| Chain | Residue | Details |
| H | HIS353 | |
| H | CYS269 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 435 |
| Chain | Residue | Details |
| B | CYS269 | covalent catalysis, proton shuttle (general acid/base) |
| A | ARG303 | electrostatic stabiliser |
| A | ARG715 | electrostatic stabiliser |
| A | GLU761 | steric role |
| A | GLN829 | metal ligand |
| A | GLU841 | metal ligand |
| A | ASN843 | metal ligand |
| A | ARG848 | electrostatic stabiliser |
| B | HIS353 | proton shuttle (general acid/base) |
| B | GLU355 | steric role |
| A | GLU215 | steric role |
| A | HIS243 | proton shuttle (general acid/base) |
| A | ASN283 | electrostatic stabiliser |
| A | GLN285 | metal ligand |
| A | GLU299 | metal ligand |
| A | ASN301 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 435 |
| Chain | Residue | Details |
| D | CYS269 | covalent catalysis, proton shuttle (general acid/base) |
| C | ARG303 | electrostatic stabiliser |
| C | ARG715 | electrostatic stabiliser |
| C | GLU761 | steric role |
| C | GLN829 | metal ligand |
| C | GLU841 | metal ligand |
| C | ASN843 | metal ligand |
| C | ARG848 | electrostatic stabiliser |
| D | HIS353 | proton shuttle (general acid/base) |
| D | GLU355 | steric role |
| C | GLU215 | steric role |
| C | HIS243 | proton shuttle (general acid/base) |
| C | ASN283 | electrostatic stabiliser |
| C | GLN285 | metal ligand |
| C | GLU299 | metal ligand |
| C | ASN301 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 435 |
| Chain | Residue | Details |
| F | CYS269 | covalent catalysis, proton shuttle (general acid/base) |
| E | ARG303 | electrostatic stabiliser |
| E | ARG715 | electrostatic stabiliser |
| E | GLU761 | steric role |
| E | GLN829 | metal ligand |
| E | GLU841 | metal ligand |
| E | ASN843 | metal ligand |
| E | ARG848 | electrostatic stabiliser |
| F | HIS353 | proton shuttle (general acid/base) |
| F | GLU355 | steric role |
| E | GLU215 | steric role |
| E | HIS243 | proton shuttle (general acid/base) |
| E | ASN283 | electrostatic stabiliser |
| E | GLN285 | metal ligand |
| E | GLU299 | metal ligand |
| E | ASN301 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 435 |
| Chain | Residue | Details |
| H | CYS269 | covalent catalysis, proton shuttle (general acid/base) |
| G | ARG303 | electrostatic stabiliser |
| G | ARG715 | electrostatic stabiliser |
| G | GLU761 | steric role |
| G | GLN829 | metal ligand |
| G | GLU841 | metal ligand |
| G | ASN843 | metal ligand |
| G | ARG848 | electrostatic stabiliser |
| H | HIS353 | proton shuttle (general acid/base) |
| H | GLU355 | steric role |
| G | GLU215 | steric role |
| G | HIS243 | proton shuttle (general acid/base) |
| G | ASN283 | electrostatic stabiliser |
| G | GLN285 | metal ligand |
| G | GLU299 | metal ligand |
| G | ASN301 | metal ligand |






