3SXP
Crystal Structure of Helicobacter pylori ADP-L-glycero-D-manno-heptose-6-epimerase (rfaD, HP0859)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0050661 | molecular_function | NADP binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0050661 | molecular_function | NADP binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0050661 | molecular_function | NADP binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0050661 | molecular_function | NADP binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0005975 | biological_process | carbohydrate metabolic process |
E | 0008712 | molecular_function | ADP-glyceromanno-heptose 6-epimerase activity |
E | 0016853 | molecular_function | isomerase activity |
E | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE NAD A 2402 |
Chain | Residue |
A | GLY17 |
A | ALA75 |
A | ASP76 |
A | ILE77 |
A | GLN97 |
A | ALA98 |
A | ALA99 |
A | ALA136 |
A | SER137 |
A | SER138 |
A | TYR161 |
A | ALA19 |
A | LYS165 |
A | TYR186 |
A | VAL189 |
A | LYS197 |
A | HOH390 |
A | HOH404 |
A | HOH412 |
A | GLY20 |
A | PHE21 |
A | VAL22 |
A | ASP43 |
A | LYS44 |
A | SER58 |
A | GLY60 |
site_id | AC2 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD B 2401 |
Chain | Residue |
B | GLY17 |
B | ALA19 |
B | GLY20 |
B | PHE21 |
B | VAL22 |
B | ASP43 |
B | LYS44 |
B | SER58 |
B | LEU59 |
B | GLY60 |
B | ALA75 |
B | ASP76 |
B | ILE77 |
B | GLN97 |
B | ALA98 |
B | ALA99 |
B | ALA136 |
B | SER137 |
B | SER138 |
B | TYR161 |
B | LYS165 |
B | TYR186 |
B | VAL189 |
B | LYS197 |
B | HOH383 |
B | HOH389 |
B | HOH403 |
site_id | AC3 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD C 2403 |
Chain | Residue |
C | GLY17 |
C | ALA19 |
C | GLY20 |
C | PHE21 |
C | VAL22 |
C | ASP43 |
C | LYS44 |
C | SER58 |
C | LEU59 |
C | GLY60 |
C | ALA75 |
C | ASP76 |
C | ILE77 |
C | GLN97 |
C | ALA98 |
C | ALA99 |
C | ALA136 |
C | SER137 |
C | SER138 |
C | TYR161 |
C | LYS165 |
C | TYR186 |
C | VAL189 |
C | LYS197 |
C | HOH369 |
C | HOH375 |
C | HOH384 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAD D 2401 |
Chain | Residue |
D | LYS165 |
D | TYR186 |
D | ASN188 |
D | VAL189 |
D | LYS197 |
D | HOH372 |
D | HOH374 |
D | HOH379 |
D | GLY17 |
D | ALA19 |
D | GLY20 |
D | PHE21 |
D | VAL22 |
D | ASP43 |
D | LYS44 |
D | SER58 |
D | GLY60 |
D | ALA75 |
D | ASP76 |
D | ILE77 |
D | GLN97 |
D | ALA98 |
D | ALA99 |
D | ALA136 |
D | SER137 |
D | SER138 |
D | TYR161 |
site_id | AC5 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE NAD E 2403 |
Chain | Residue |
E | GLY17 |
E | ALA19 |
E | GLY20 |
E | PHE21 |
E | VAL22 |
E | ASP43 |
E | LYS44 |
E | SER58 |
E | GLY60 |
E | ALA75 |
E | ASP76 |
E | ILE77 |
E | GLN97 |
E | ALA98 |
E | ALA99 |
E | ALA136 |
E | SER137 |
E | SER138 |
E | TYR161 |
E | LYS165 |
E | TYR186 |
E | VAL189 |
E | LYS197 |
E | HOH379 |
E | HOH384 |