1RYW
C115S MurA liganded with reaction products
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 | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2461 |
| Chain | Residue |
| A | LYS22 |
| A | ARG120 |
| A | ARG397 |
| A | HOH682 |
| A | HOH761 |
| A | HOH810 |
| A | EPU2450 |
| A | GOL2471 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 3461 |
| Chain | Residue |
| B | ARG120 |
| B | ARG397 |
| B | HOH621 |
| B | HOH1332 |
| B | EPU3450 |
| B | GOL3471 |
| B | LYS22 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C 4461 |
| Chain | Residue |
| C | LYS22 |
| C | ARG120 |
| C | ARG397 |
| C | HOH1146 |
| C | HOH1633 |
| C | EPU4450 |
| C | GOL4471 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 D 5461 |
| Chain | Residue |
| D | LYS22 |
| D | ARG120 |
| D | HOH452 |
| D | EPU5450 |
| D | GOL5471 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 E 6461 |
| Chain | Residue |
| E | LYS22 |
| E | ARG120 |
| E | ARG397 |
| E | HOH583 |
| E | HOH752 |
| E | EPU6450 |
| E | GOL6471 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 F 7461 |
| Chain | Residue |
| F | LYS22 |
| F | ARG120 |
| F | HOH424 |
| F | EPU7450 |
| F | GOL7471 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 G 8461 |
| Chain | Residue |
| G | LYS22 |
| G | ARG120 |
| G | ARG397 |
| G | HOH436 |
| G | HOH1037 |
| G | EPU8450 |
| G | GOL8471 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 G 8462 |
| Chain | Residue |
| G | GLY114 |
| G | SER115 |
| G | ALA116 |
| G | HOH438 |
| H | MET366 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 H 9461 |
| Chain | Residue |
| H | LYS22 |
| H | ARG120 |
| H | ARG397 |
| H | HOH567 |
| H | EPU9450 |
| H | GOL9471 |
| site_id | BC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE EPU E 6450 |
| Chain | Residue |
| E | LYS22 |
| 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 | ARG331 |
| E | ARG371 |
| E | HOH424 |
| E | HOH425 |
| E | HOH431 |
| E | HOH433 |
| E | HOH436 |
| E | HOH438 |
| E | HOH465 |
| E | HOH596 |
| E | HOH756 |
| E | HOH798 |
| E | PO46461 |
| E | GOL6471 |
| site_id | BC2 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE EPU B 3450 |
| Chain | Residue |
| B | GLY164 |
| B | THR304 |
| B | ASP305 |
| B | ILE327 |
| B | PHE328 |
| B | ARG331 |
| B | ARG371 |
| B | HOH422 |
| B | HOH430 |
| B | HOH431 |
| B | HOH434 |
| B | HOH445 |
| B | HOH451 |
| B | HOH452 |
| B | HOH458 |
| B | HOH472 |
| B | HOH658 |
| B | HOH917 |
| B | HOH1438 |
| B | PO43461 |
| B | GOL3471 |
| B | LYS22 |
| B | ASN23 |
| B | TRP95 |
| B | ARG120 |
| B | PRO121 |
| B | VAL122 |
| B | ASP123 |
| B | LEU124 |
| B | LYS160 |
| B | SER162 |
| B | VAL163 |
| site_id | BC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE EPU C 4450 |
| Chain | Residue |
| C | LYS22 |
| C | ASN23 |
| C | TRP95 |
| C | ARG120 |
| C | PRO121 |
| C | VAL122 |
| C | ASP123 |
| C | LEU124 |
| C | HIS125 |
| C | LYS160 |
| C | SER162 |
| C | VAL163 |
| C | GLY164 |
| C | THR304 |
| C | ASP305 |
| C | ILE327 |
| C | PHE328 |
| C | ARG331 |
| C | ARG371 |
| C | HOH420 |
| C | HOH421 |
| C | HOH424 |
| C | HOH425 |
| C | HOH433 |
| C | HOH445 |
| C | HOH459 |
| C | HOH522 |
| C | HOH592 |
| C | PO44461 |
| C | GOL4471 |
| site_id | BC4 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE EPU D 5450 |
| Chain | Residue |
| D | LYS22 |
| 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 | ARG331 |
| D | ARG371 |
| D | HOH427 |
| D | HOH438 |
| D | HOH444 |
| D | HOH448 |
| D | HOH451 |
| D | HOH459 |
| D | HOH464 |
| D | HOH473 |
| D | HOH641 |
| D | HOH703 |
| D | HOH1114 |
| D | PO45461 |
| D | GOL5471 |
| site_id | BC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE EPU A 2450 |
| Chain | Residue |
| A | LYS22 |
| A | ASN23 |
| A | TRP95 |
| A | ARG120 |
| A | PRO121 |
| A | VAL122 |
| A | ASP123 |
| A | LEU124 |
| A | HIS125 |
| A | LYS160 |
| A | SER162 |
| A | VAL163 |
| A | GLY164 |
| A | THR304 |
| A | ASP305 |
| A | ILE327 |
| A | PHE328 |
| A | ARG331 |
| A | ARG371 |
| A | HOH422 |
| A | HOH425 |
| A | HOH429 |
| A | HOH432 |
| A | HOH439 |
| A | HOH454 |
| A | HOH462 |
| A | HOH465 |
| A | HOH667 |
| A | HOH1742 |
| A | HOH1766 |
| A | PO42461 |
| A | GOL2471 |
| site_id | BC6 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE EPU F 7450 |
| Chain | Residue |
| F | LYS22 |
| 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 | ARG331 |
| F | ARG371 |
| F | HOH420 |
| F | HOH427 |
| F | HOH429 |
| F | HOH447 |
| F | HOH465 |
| F | HOH580 |
| F | HOH912 |
| F | HOH1101 |
| F | HOH1171 |
| F | PO47461 |
| F | GOL7471 |
| site_id | BC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE EPU G 8450 |
| Chain | Residue |
| G | LYS22 |
| G | ASN23 |
| G | TRP95 |
| G | ARG120 |
| G | PRO121 |
| G | VAL122 |
| G | ASP123 |
| G | LEU124 |
| G | HIS125 |
| G | LYS160 |
| G | SER162 |
| G | VAL163 |
| G | GLY164 |
| G | THR304 |
| G | ASP305 |
| G | ILE327 |
| G | PHE328 |
| G | ARG331 |
| G | ARG371 |
| G | HOH420 |
| G | HOH425 |
| G | HOH426 |
| G | HOH462 |
| G | HOH476 |
| G | HOH481 |
| G | HOH485 |
| G | HOH492 |
| G | HOH532 |
| G | HOH1354 |
| G | PO48461 |
| G | GOL8471 |
| site_id | BC8 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE EPU H 9450 |
| Chain | Residue |
| H | LYS22 |
| H | ASN23 |
| H | TRP95 |
| H | ARG120 |
| H | PRO121 |
| H | VAL122 |
| H | ASP123 |
| H | LEU124 |
| H | HIS125 |
| H | LYS160 |
| H | SER162 |
| H | VAL163 |
| H | GLY164 |
| H | THR304 |
| H | ASP305 |
| H | ILE327 |
| H | PHE328 |
| H | ARG331 |
| H | ARG371 |
| H | HOH434 |
| H | HOH440 |
| H | HOH443 |
| H | HOH446 |
| H | HOH447 |
| H | HOH461 |
| H | HOH467 |
| H | HOH472 |
| H | HOH509 |
| H | HOH934 |
| H | PO49461 |
| H | GOL9471 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 2471 |
| Chain | Residue |
| A | ARG91 |
| A | ALA92 |
| A | ILE94 |
| A | TRP95 |
| A | HIS125 |
| A | GLY164 |
| A | HOH429 |
| A | EPU2450 |
| A | PO42461 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 2472 |
| Chain | Residue |
| A | ARG252 |
| A | TRP279 |
| A | HOH1610 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 2473 |
| Chain | Residue |
| A | TYR393 |
| C | ARG391 |
| site_id | CC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 3471 |
| Chain | Residue |
| B | ARG91 |
| B | ALA92 |
| B | TRP95 |
| B | HIS125 |
| B | GLY164 |
| B | HOH430 |
| B | HOH621 |
| B | EPU3450 |
| B | PO43461 |
| site_id | CC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL B 3472 |
| Chain | Residue |
| B | ARG252 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 3473 |
| Chain | Residue |
| A | ARG391 |
| C | TYR393 |
| site_id | CC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 4471 |
| Chain | Residue |
| C | ARG91 |
| C | ILE94 |
| C | TRP95 |
| C | ARG120 |
| C | HIS125 |
| C | HOH420 |
| C | EPU4450 |
| C | PO44461 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL C 4472 |
| Chain | Residue |
| C | ARG252 |
| C | HOH1648 |
| site_id | CC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 4474 |
| Chain | Residue |
| A | GLU329 |
| A | HOH1435 |
| C | GLU325 |
| C | PHE328 |
| C | GLU329 |
| C | ASN330 |
| C | ARG331 |
| C | PHE332 |
| C | HOH625 |
| site_id | CC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 5471 |
| Chain | Residue |
| D | ARG91 |
| D | ALA92 |
| D | ILE94 |
| D | ARG120 |
| D | HIS125 |
| D | GLY164 |
| D | HOH427 |
| D | EPU5450 |
| D | PO45461 |
| site_id | DC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 5472 |
| Chain | Residue |
| D | VAL250 |
| D | ARG252 |
| D | HOH1290 |
| site_id | DC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL E 6471 |
| Chain | Residue |
| E | ARG91 |
| E | ALA92 |
| E | ILE94 |
| E | TRP95 |
| E | HIS125 |
| E | GLY164 |
| E | HOH425 |
| E | EPU6450 |
| E | PO46461 |
| site_id | DC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL F 7471 |
| Chain | Residue |
| F | ARG91 |
| F | ALA92 |
| F | ILE94 |
| F | TRP95 |
| F | ARG120 |
| F | HIS125 |
| F | GLY164 |
| F | HOH447 |
| F | EPU7450 |
| F | PO47461 |
| site_id | DC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL G 8471 |
| Chain | Residue |
| G | ARG91 |
| G | ALA92 |
| G | TRP95 |
| G | HIS125 |
| G | GLY164 |
| G | HOH420 |
| G | EPU8450 |
| G | PO48461 |
| site_id | DC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL E 8472 |
| Chain | Residue |
| E | ARG252 |
| site_id | DC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL H 9471 |
| Chain | Residue |
| H | ARG91 |
| H | ILE94 |
| H | TRP95 |
| H | ARG120 |
| H | HIS125 |
| H | GLY164 |
| H | EPU9450 |
| H | PO49461 |
| site_id | DC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL H 9472 |
| Chain | Residue |
| H | VAL250 |
| H | ARG252 |
| H | TRP279 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20392080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LTH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20392080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LTH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"2-(S-cysteinyl)pyruvic acid O-phosphothioketal","evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| A | ASP305 | |
| A | ARG397 | |
| A | SER115 | |
| A | ASN23 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| B | ASP305 | |
| B | ARG397 | |
| B | SER115 | |
| B | ASN23 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| C | ASP305 | |
| C | ARG397 | |
| C | SER115 | |
| C | ASN23 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| D | ASP305 | |
| D | ARG397 | |
| D | SER115 | |
| D | ASN23 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| E | ASP305 | |
| E | ARG397 | |
| E | SER115 | |
| E | ASN23 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| F | ASP305 | |
| F | ARG397 | |
| F | SER115 | |
| F | ASN23 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| G | ASP305 | |
| G | ARG397 | |
| G | SER115 | |
| G | ASN23 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| H | ASP305 | |
| H | ARG397 | |
| H | SER115 | |
| H | ASN23 |
| 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 | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| A | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG401 | 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 | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| B | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| B | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG401 | 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 | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| C | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| C | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ARG401 | 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 | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| D | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| D | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ARG401 | 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 | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| E | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| E | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | ARG401 | 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 | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| F | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| F | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | ARG401 | 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 | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| G | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| G | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| G | ARG401 | 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 | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| H | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| H | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| H | ARG401 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |






