3VCY
Structure of MurA (UDP-N-acetylglucosamine enolpyruvyl transferase), from Vibrio fischeri in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin.
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 | 7 |
Details | BINDING SITE FOR RESIDUE FFQ A 500 |
Chain | Residue |
A | CYS116 |
A | ARG121 |
A | ARG398 |
A | PO4502 |
A | HOH614 |
A | HOH617 |
A | HOH876 |
site_id | AC2 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE UD1 A 501 |
Chain | Residue |
A | ALA120 |
A | ARG121 |
A | PRO122 |
A | VAL123 |
A | ASP124 |
A | LEU125 |
A | HIS126 |
A | SER163 |
A | VAL164 |
A | GLY165 |
A | THR305 |
A | ASP306 |
A | ILE328 |
A | PHE329 |
A | ARG332 |
A | PO4502 |
A | GOL503 |
A | HOH603 |
A | HOH611 |
A | HOH613 |
A | HOH634 |
A | HOH648 |
A | HOH670 |
A | HOH804 |
A | HOH844 |
A | HOH868 |
A | HOH875 |
A | ASN24 |
A | TRP96 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 A 502 |
Chain | Residue |
A | LYS23 |
A | ARG121 |
A | ARG398 |
A | FFQ500 |
A | UD1501 |
A | GOL503 |
A | HOH617 |
A | HOH618 |
A | HOH781 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 503 |
Chain | Residue |
A | ARG92 |
A | ALA93 |
A | ILE95 |
A | HIS126 |
A | GLY165 |
A | UD1501 |
A | PO4502 |
A | HOH613 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FFQ B 500 |
Chain | Residue |
B | ARG92 |
B | CYS116 |
B | ARG121 |
B | ARG398 |
B | HOH760 |
B | HOH850 |
site_id | AC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE UD1 B 501 |
Chain | Residue |
B | LYS23 |
B | ASN24 |
B | TRP96 |
B | ALA120 |
B | ARG121 |
B | PRO122 |
B | VAL123 |
B | ASP124 |
B | LEU125 |
B | HIS126 |
B | SER163 |
B | VAL164 |
B | GLY165 |
B | THR305 |
B | ASP306 |
B | ILE328 |
B | PHE329 |
B | PO4502 |
B | GOL503 |
B | HOH611 |
B | HOH618 |
B | HOH619 |
B | HOH632 |
B | HOH685 |
B | HOH695 |
B | HOH712 |
B | HOH746 |
B | HOH786 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 B 502 |
Chain | Residue |
B | LYS23 |
B | ARG121 |
B | UD1501 |
B | GOL503 |
B | HOH604 |
B | HOH727 |
B | HOH853 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 503 |
Chain | Residue |
B | UD1501 |
B | PO4502 |
B | HOH611 |
B | ARG92 |
B | ALA93 |
B | ILE95 |
B | TRP96 |
B | GLY165 |
site_id | AC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE FFQ C 500 |
Chain | Residue |
C | ARG92 |
C | GLY115 |
C | CYS116 |
C | ARG121 |
C | ARG398 |
C | PO4502 |
C | HOH673 |
C | HOH756 |
C | HOH859 |
C | HOH877 |
C | HOH898 |
site_id | BC1 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE UD1 C 501 |
Chain | Residue |
C | ASN24 |
C | TRP96 |
C | ALA120 |
C | ARG121 |
C | PRO122 |
C | VAL123 |
C | ASP124 |
C | LEU125 |
C | HIS126 |
C | SER163 |
C | VAL164 |
C | GLY165 |
C | THR305 |
C | ASP306 |
C | ILE328 |
C | PHE329 |
C | PO4502 |
C | GOL503 |
C | HOH614 |
C | HOH625 |
C | HOH626 |
C | HOH627 |
C | HOH629 |
C | HOH630 |
C | HOH828 |
C | HOH876 |
C | HOH896 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 C 502 |
Chain | Residue |
C | LYS23 |
C | ARG121 |
C | FFQ500 |
C | UD1501 |
C | GOL503 |
C | HOH736 |
C | HOH862 |
C | HOH895 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 503 |
Chain | Residue |
C | ARG92 |
C | ALA93 |
C | ILE95 |
C | HIS126 |
C | GLY165 |
C | UD1501 |
C | PO4502 |
C | HOH629 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FFQ D 500 |
Chain | Residue |
D | ARG92 |
D | CYS116 |
D | ARG121 |
D | ARG398 |
D | HOH602 |
D | HOH661 |
D | HOH920 |
site_id | BC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE UD1 D 501 |
Chain | Residue |
D | ASN24 |
D | TRP96 |
D | ALA120 |
D | ARG121 |
D | PRO122 |
D | VAL123 |
D | ASP124 |
D | LEU125 |
D | HIS126 |
D | SER163 |
D | VAL164 |
D | GLY165 |
D | THR305 |
D | ASP306 |
D | ILE328 |
D | PHE329 |
D | PO4502 |
D | GOL503 |
D | HOH616 |
D | HOH617 |
D | HOH621 |
D | HOH622 |
D | HOH629 |
D | HOH818 |
D | HOH849 |
D | HOH922 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 D 502 |
Chain | Residue |
D | LYS23 |
D | ARG121 |
D | ARG398 |
D | UD1501 |
D | GOL503 |
D | HOH601 |
D | HOH603 |
D | HOH716 |
D | HOH918 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 503 |
Chain | Residue |
D | ARG92 |
D | ALA93 |
D | ILE95 |
D | ARG121 |
D | GLY165 |
D | UD1501 |
D | PO4502 |
D | HOH622 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00111 |
Chain | Residue | Details |
A | CYS116 | |
B | CYS116 | |
C | CYS116 | |
D | CYS116 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:22505403, ECO:0007744|PDB:3VCY |
Chain | Residue | Details |
A | LYS23 | |
A | LYS161 | |
B | LYS23 | |
B | LYS161 | |
C | LYS23 | |
C | LYS161 | |
D | LYS23 | |
D | LYS161 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
Chain | Residue | Details |
A | ARG92 | |
B | ARG92 | |
C | ARG92 | |
D | ARG92 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22505403, ECO:0007744|PDB:3VCY |
Chain | Residue | Details |
A | ARG121 | |
D | ARG121 | |
D | ASP306 | |
D | ILE328 | |
A | ASP306 | |
A | ILE328 | |
B | ARG121 | |
B | ASP306 | |
B | ILE328 | |
C | ARG121 | |
C | ASP306 | |
C | ILE328 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111 |
Chain | Residue | Details |
A | CYS116 | |
B | CYS116 | |
C | CYS116 | |
D | CYS116 |