4ZAS
Crystal structure of sugar aminotransferase CalS13 from Micromonospora echinospora
Replaces: 4YTJFunctional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000271 | biological_process | polysaccharide biosynthetic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0000271 | biological_process | polysaccharide biosynthetic process |
B | 0008483 | molecular_function | transaminase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0000271 | biological_process | polysaccharide biosynthetic process |
C | 0008483 | molecular_function | transaminase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0000271 | biological_process | polysaccharide biosynthetic process |
D | 0008483 | molecular_function | transaminase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
E | 0000271 | biological_process | polysaccharide biosynthetic process |
E | 0008483 | molecular_function | transaminase activity |
E | 0030170 | molecular_function | pyridoxal phosphate binding |
F | 0000271 | biological_process | polysaccharide biosynthetic process |
F | 0008483 | molecular_function | transaminase activity |
F | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 401 |
Chain | Residue |
B | PRO19 |
B | ARG267 |
site_id | AC2 |
Number of Residues | 14 |
Details | binding site for residue T46 B 402 |
Chain | Residue |
B | ARG33 |
B | LEU34 |
B | GLU35 |
B | TRP228 |
B | ARG233 |
B | ARG237 |
B | HOH513 |
A | SER13 |
A | VAL15 |
A | PHE96 |
A | ALA200 |
A | ILE201 |
A | LLP202 |
B | GLY32 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 401 |
Chain | Residue |
C | ARG55 |
C | ASP216 |
C | ASP217 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue TYD D 500 |
Chain | Residue |
C | SER13 |
C | ALA200 |
C | ILE201 |
D | GLY32 |
D | ARG33 |
D | LEU34 |
D | GLU35 |
D | TRP228 |
D | ARG233 |
D | ARG237 |
D | HOH632 |
D | HOH644 |
D | HOH668 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue TYD E 500 |
Chain | Residue |
E | GLY32 |
E | ARG33 |
E | LEU34 |
E | GLU35 |
E | TRP228 |
E | ARG233 |
E | ARG237 |
E | HOH605 |
F | VAL15 |
F | ILE201 |
site_id | AC6 |
Number of Residues | 14 |
Details | binding site for residue TYD F 500 |
Chain | Residue |
E | VAL15 |
E | ALA200 |
E | ILE201 |
F | GLY32 |
F | ARG33 |
F | LEU34 |
F | GLU35 |
F | TRP228 |
F | ARG233 |
F | ARG237 |
F | HOH606 |
F | HOH621 |
F | HOH632 |
F | HOH634 |