1EJD
Crystal structure of unliganded mura (type1)
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2422 |
| Chain | Residue |
| B | ASN23 |
| B | ASP305 |
| B | ARG371 |
| B | HOH423 |
| B | HOH741 |
| B | HOH808 |
| B | HOH832 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2424 |
| Chain | Residue |
| B | GLY164 |
| B | HOH425 |
| B | HOH428 |
| B | HOH480 |
| B | HOH838 |
| B | PO42427 |
| B | SER162 |
| B | VAL163 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2425 |
| Chain | Residue |
| B | HIS155 |
| B | GLY319 |
| B | THR320 |
| B | HOH596 |
| B | HOH729 |
| B | PO42428 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2426 |
| Chain | Residue |
| B | ALA119 |
| B | ASP159 |
| B | HOH825 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2427 |
| Chain | Residue |
| B | PRO121 |
| B | SER162 |
| B | HOH425 |
| B | HOH917 |
| B | PO42424 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2428 |
| Chain | Residue |
| B | GLY319 |
| B | THR320 |
| B | HIS355 |
| B | HOH588 |
| B | PO42425 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2429 |
| Chain | Residue |
| B | ARG401 |
| B | GLU403 |
| B | ARG407 |
| B | ARG415 |
| B | HOH692 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2430 |
| Chain | Residue |
| A | GLU274 |
| A | HOH715 |
| B | GLY14 |
| B | GLU15 |
| B | HAI1422 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2431 |
| Chain | Residue |
| A | GLU188 |
| A | ARG232 |
| A | HIS299 |
| A | PRO303 |
| A | HOH444 |
| A | HOH552 |
| A | HOH590 |
| A | HOH815 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2432 |
| Chain | Residue |
| A | GLU135 |
| A | LYS137 |
| A | HOH421 |
| A | HOH426 |
| A | HOH426 |
| A | HOH435 |
| A | HOH919 |
| A | HAI1424 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2433 |
| Chain | Residue |
| A | ARG252 |
| A | ASP278 |
| B | ARG252 |
| B | ASN253 |
| B | HAI1420 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2434 |
| Chain | Residue |
| A | ARG401 |
| A | GLU403 |
| A | ASP404 |
| A | ARG407 |
| A | ARG415 |
| A | HOH728 |
| A | HOH748 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2436 |
| Chain | Residue |
| A | HIS394 |
| A | ARG397 |
| A | HOH592 |
| A | HOH633 |
| A | HOH648 |
| A | HOH895 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2437 |
| Chain | Residue |
| A | SER162 |
| A | VAL163 |
| A | GLY164 |
| A | HOH423 |
| A | HOH428 |
| A | HOH431 |
| A | HOH764 |
| A | HOH912 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 2439 |
| Chain | Residue |
| B | ASP193 |
| B | ASN196 |
| B | TYR226 |
| B | GLN255 |
| B | HOH420 |
| B | HOH549 |
| B | HOH551 |
| B | HOH564 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HAI B 1420 |
| Chain | Residue |
| B | HOH427 |
| A | VAL250 |
| A | TRP279 |
| A | PO42433 |
| B | VAL250 |
| B | TRP279 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HAI B 1421 |
| Chain | Residue |
| B | GLU65 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HAI B 1422 |
| Chain | Residue |
| A | VAL250 |
| A | GLU274 |
| A | PO42430 |
| B | VAL250 |
| B | GLU274 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HAI A 1424 |
| Chain | Residue |
| A | PHE80 |
| A | GLN108 |
| A | GLU135 |
| A | ASN148 |
| A | PO42432 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| 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 | 2 |
| 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 | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| 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 | 6 |
| 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 | 2 |
| 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 | CYS115 | |
| 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 | CYS115 | |
| B | 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 |
