4HDR
Crystal Structure of ArsAB in Complex with 5,6-dimethylbenzimidazole
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008939 | molecular_function | nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity |
A | 0009236 | biological_process | cobalamin biosynthetic process |
A | 0016757 | molecular_function | glycosyltransferase activity |
B | 0008939 | molecular_function | nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity |
B | 0009236 | biological_process | cobalamin biosynthetic process |
B | 0016757 | molecular_function | glycosyltransferase activity |
C | 0008939 | molecular_function | nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity |
C | 0009236 | biological_process | cobalamin biosynthetic process |
C | 0016757 | molecular_function | glycosyltransferase activity |
D | 0008939 | molecular_function | nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity |
D | 0009236 | biological_process | cobalamin biosynthetic process |
D | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE DMD A 801 |
Chain | Residue |
A | TYR79 |
B | PHE327 |
A | THR83 |
A | MET87 |
A | MET177 |
A | LEU317 |
A | GLU319 |
A | HOH901 |
B | LYS29 |
B | PRO30 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 802 |
Chain | Residue |
A | GLY178 |
A | GLY180 |
A | ASN181 |
A | THR182 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 401 |
Chain | Residue |
A | PHE105 |
B | HIS319 |
B | EDO405 |
B | HOH520 |
B | HOH605 |
B | HOH811 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 402 |
Chain | Residue |
A | HOH1053 |
B | PHE276 |
B | ALA277 |
B | ALA278 |
B | GLN296 |
B | LEU297 |
B | LYS298 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 403 |
Chain | Residue |
B | ILE160 |
B | HOH601 |
D | HIS39 |
D | HOH521 |
D | HOH658 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 404 |
Chain | Residue |
B | ARG124 |
B | LYS125 |
B | LYS126 |
B | HOH537 |
B | HOH666 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 405 |
Chain | Residue |
A | PHE105 |
A | ASP328 |
B | HIS100 |
B | VAL101 |
B | SER312 |
B | ASN315 |
B | EDO401 |
B | HOH674 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE DMD C 801 |
Chain | Residue |
C | TYR79 |
C | THR83 |
C | MET87 |
C | MET177 |
C | LEU317 |
C | GLU319 |
C | HOH904 |
D | LYS29 |
D | PRO30 |
D | PHE327 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 802 |
Chain | Residue |
C | GLY178 |
C | GLY180 |
C | ASN181 |
C | THR182 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO C 803 |
Chain | Residue |
C | GLU176 |
C | ASP265 |
C | GLY266 |
C | LEU267 |
C | ASN268 |
C | THR269 |
C | GLY318 |
C | HOH905 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 401 |
Chain | Residue |
C | PHE105 |
D | HIS319 |
D | EDO404 |
D | HOH594 |
D | HOH750 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 402 |
Chain | Residue |
D | PHE276 |
D | LEU286 |
D | VAL291 |
D | PRO292 |
D | ALA293 |
D | HOH513 |
D | HOH514 |
D | HOH591 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO D 403 |
Chain | Residue |
C | HOH986 |
D | PHE276 |
D | ALA277 |
D | ALA278 |
D | GLN296 |
D | LEU297 |
D | LYS298 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 404 |
Chain | Residue |
C | PHE105 |
C | ASP328 |
D | HIS100 |
D | VAL101 |
D | SER312 |
D | ASN315 |
D | EDO401 |
D | HOH687 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 405 |
Chain | Residue |
D | ILE261 |
D | LEU288 |
D | LEU289 |
D | ASP290 |
B | ASN50 |
B | ARG54 |
B | HOH592 |
B | HOH632 |