1ZHQ
Crystal structure of apo MVL
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0050688 | biological_process | regulation of defense response to virus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0050688 | biological_process | regulation of defense response to virus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| C | 0030246 | molecular_function | carbohydrate binding |
| C | 0050688 | biological_process | regulation of defense response to virus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| D | 0030246 | molecular_function | carbohydrate binding |
| D | 0050688 | biological_process | regulation of defense response to virus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| E | 0030246 | molecular_function | carbohydrate binding |
| E | 0050688 | biological_process | regulation of defense response to virus |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| F | 0030246 | molecular_function | carbohydrate binding |
| F | 0050688 | biological_process | regulation of defense response to virus |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| G | 0030246 | molecular_function | carbohydrate binding |
| G | 0050688 | biological_process | regulation of defense response to virus |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| H | 0030246 | molecular_function | carbohydrate binding |
| H | 0050688 | biological_process | regulation of defense response to virus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 A 901 |
| Chain | Residue |
| A | LYS63 |
| A | LYS110 |
| A | HOH1060 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 902 |
| Chain | Residue |
| A | HOH1041 |
| B | GLU76 |
| B | LYS79 |
| B | LEU80 |
| B | HOH1116 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 B 903 |
| Chain | Residue |
| B | HOH1065 |
| B | GLU61 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 904 |
| Chain | Residue |
| B | LYS63 |
| B | LYS110 |
| B | HOH1103 |
| E | LYS4 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 D 905 |
| Chain | Residue |
| D | GLU91 |
| D | LYS110 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 F 906 |
| Chain | Residue |
| F | ASP65 |
| F | ARG97 |
| F | GLN108 |
| H | TRP37 |
| H | THR38 |
| H | HOH1016 |
| H | HOH1021 |
| H | HOH1093 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO E 1001 |
| Chain | Residue |
| E | GLU55 |
| E | ASN56 |
| E | GLY89 |
| E | ALA90 |
| E | HOH1047 |
| E | HOH1057 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO F 1002 |
| Chain | Residue |
| F | HIS29 |
| F | SER87 |
| F | TYR88 |
| F | HOH1015 |
| F | HOH1018 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO E 1003 |
| Chain | Residue |
| E | HIS29 |
| E | SER87 |
| E | TYR88 |
| E | HOH1005 |
| E | HOH1012 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1004 |
| Chain | Residue |
| A | HIS29 |
| A | SER87 |
| A | TYR88 |
| A | HOH1013 |
| A | HOH1025 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1005 |
| Chain | Residue |
| A | PRO8 |
| B | HIS29 |
| B | SER87 |
| B | HOH1015 |
| B | HOH1028 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 1006 |
| Chain | Residue |
| C | HIS29 |
| C | SER87 |
| C | TYR88 |
| C | HOH1010 |
| C | HOH1015 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 1007 |
| Chain | Residue |
| C | PRO8 |
| D | HIS29 |
| D | LEU52 |
| D | SER87 |
| D | TYR88 |
| D | HOH1021 |
| D | HOH1025 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO F 1008 |
| Chain | Residue |
| F | VAL54 |
| F | GLU55 |
| F | ASN56 |
| F | GLY89 |
| F | ALA90 |
| F | HOH1017 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 1009 |
| Chain | Residue |
| B | ASP65 |
| B | TRP96 |
| B | ARG97 |
| E | GLN36 |
| E | TRP37 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO G 1010 |
| Chain | Residue |
| G | HIS29 |
| G | LEU52 |
| G | SER87 |
| G | HOH1014 |
| G | HOH1021 |
| G | HOH1099 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO H 1011 |
| Chain | Residue |
| G | LEU67 |
| G | TYR88 |
| H | ALA28 |
| H | HIS29 |
| H | GLN30 |
| H | TYR88 |
| H | TYR111 |
| H | HOH1018 |
| H | HOH1019 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 1012 |
| Chain | Residue |
| B | ARG97 |
| B | HOH1109 |
| E | ASN15 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 1013 |
| Chain | Residue |
| B | PRO70 |
| B | LEU71 |
| B | GLU101 |
| B | GLY102 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PRO11 | |
| B | PRO70 | |
| B | GLN78 | |
| B | GLY94 | |
| C | PRO11 | |
| C | GLN19 | |
| C | GLY35 | |
| C | PRO70 | |
| C | GLN78 | |
| C | GLY94 | |
| D | PRO11 | |
| A | GLN19 | |
| D | GLN19 | |
| D | GLY35 | |
| D | PRO70 | |
| D | GLN78 | |
| D | GLY94 | |
| E | PRO11 | |
| E | GLN19 | |
| E | GLY35 | |
| E | PRO70 | |
| E | GLN78 | |
| A | GLY35 | |
| E | GLY94 | |
| F | PRO11 | |
| F | GLN19 | |
| F | GLY35 | |
| F | PRO70 | |
| F | GLN78 | |
| F | GLY94 | |
| G | PRO11 | |
| G | GLN19 | |
| G | GLY35 | |
| A | PRO70 | |
| G | PRO70 | |
| G | GLN78 | |
| G | GLY94 | |
| H | PRO11 | |
| H | GLN19 | |
| H | GLY35 | |
| H | PRO70 | |
| H | GLN78 | |
| H | GLY94 | |
| A | GLN78 | |
| A | GLY94 | |
| B | PRO11 | |
| B | GLN19 | |
| B | GLY35 |
