2PDO
Crystal Structure of the Putative Acetyltransferase of GNAT Family from Shigella flexneri
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
C | 0016746 | molecular_function | acyltransferase activity |
C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
D | 0016746 | molecular_function | acyltransferase activity |
D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
E | 0016746 | molecular_function | acyltransferase activity |
E | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
F | 0016746 | molecular_function | acyltransferase activity |
F | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
G | 0016746 | molecular_function | acyltransferase activity |
G | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
H | 0016746 | molecular_function | acyltransferase activity |
H | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN B 601 |
Chain | Residue |
B | GLU124 |
B | HIS125 |
B | HOH625 |
B | HOH628 |
H | GLU124 |
H | HIS125 |
H | HOH618 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN E 602 |
Chain | Residue |
E | GLU124 |
E | HIS125 |
E | HOH619 |
E | HOH638 |
E | HOH661 |
D | GLU124 |
D | HIS125 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN G 603 |
Chain | Residue |
G | ASP127 |
G | HOH610 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 604 |
Chain | Residue |
B | GLU9 |
B | GLU12 |
B | GLU13 |
B | HOH661 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN H 605 |
Chain | Residue |
G | ASP127 |
G | HOH627 |
G | HOH654 |
H | GLU109 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO D 608 |
Chain | Residue |
D | VAL74 |
D | PHE78 |
D | ARG79 |
D | GLY80 |
D | ARG81 |
D | GLY82 |
D | ILE83 |
D | ALA84 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO F 609 |
Chain | Residue |
E | ASP63 |
F | LYS37 |
F | HIS40 |
F | ASP41 |
F | LEU44 |
F | GLY61 |
F | TYR62 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO F 610 |
Chain | Residue |
F | VAL74 |
F | HOH635 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO H 611 |
Chain | Residue |
A | HOH216 |
B | ASP127 |
G | HOH668 |
H | HIS125 |
H | ASP127 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO F 612 |
Chain | Residue |
F | VAL114 |
F | TYR118 |
F | HOH673 |
F | HOH686 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO H 613 |
Chain | Residue |
H | MSE117 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO E 614 |
Chain | Residue |
E | TRP27 |
E | ARG134 |
F | ARG66 |
F | LYS102 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACY H 606 |
Chain | Residue |
G | LYS102 |
H | TRP27 |
H | ARG134 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACY B 607 |
Chain | Residue |
A | ASP63 |
B | LYS37 |
B | HIS40 |
B | ASP41 |
B | GLY61 |
B | TYR62 |
B | HOH609 |
B | HOH615 |