6JC8
Crystal structure of aminotransferase CrmG from Actinoalloteichus sp. WH1-2216-6 in complex with amino donor L-Glu
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008483 | molecular_function | transaminase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0042802 | molecular_function | identical protein binding |
B | 0008483 | molecular_function | transaminase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0042802 | molecular_function | identical protein binding |
C | 0008483 | molecular_function | transaminase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0042802 | molecular_function | identical protein binding |
D | 0008483 | molecular_function | transaminase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue PL6 A 601 |
Chain | Residue |
A | PHE55 |
A | VAL317 |
A | GLN318 |
A | LYS344 |
A | HOH702 |
A | HOH727 |
A | HOH779 |
A | HOH814 |
B | SER372 |
B | SER373 |
B | THR374 |
A | SER119 |
B | HOH722 |
A | GLY120 |
A | ALA121 |
A | ASN124 |
A | PHE207 |
A | HIS208 |
A | GLU282 |
A | ASP315 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL A 602 |
Chain | Residue |
A | ARG197 |
A | ALA229 |
A | SER231 |
B | ARG197 |
B | SER231 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue PL6 B 601 |
Chain | Residue |
A | SER372 |
A | SER373 |
A | THR374 |
B | PHE55 |
B | SER119 |
B | GLY120 |
B | ALA121 |
B | PHE207 |
B | HIS208 |
B | GLU282 |
B | ASP315 |
B | VAL317 |
B | GLN318 |
B | LYS344 |
B | HOH728 |
B | HOH738 |
B | HOH758 |
B | HOH765 |
B | HOH821 |
B | HOH835 |
site_id | AC4 |
Number of Residues | 20 |
Details | binding site for residue PL6 C 601 |
Chain | Residue |
C | PHE55 |
C | SER119 |
C | GLY120 |
C | ALA121 |
C | PHE207 |
C | HIS208 |
C | GLU282 |
C | ASP315 |
C | VAL317 |
C | GLN318 |
C | LYS344 |
C | HOH701 |
C | HOH711 |
C | HOH777 |
C | HOH786 |
C | HOH797 |
C | HOH816 |
D | SER372 |
D | SER373 |
D | THR374 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue GOL C 602 |
Chain | Residue |
C | ALA229 |
C | LEU230 |
C | SER231 |
D | ARG197 |
D | ALA229 |
D | SER231 |
D | SER232 |
site_id | AC6 |
Number of Residues | 19 |
Details | binding site for residue PL6 D 601 |
Chain | Residue |
C | SER372 |
C | THR374 |
C | HOH732 |
D | PHE55 |
D | SER119 |
D | GLY120 |
D | ALA121 |
D | PHE207 |
D | HIS208 |
D | GLU282 |
D | ASP315 |
D | VAL317 |
D | GLN318 |
D | LYS344 |
D | HOH714 |
D | HOH762 |
D | HOH779 |
D | HOH800 |
D | HOH815 |