4NF1
Structure of N-acetyltransferase domain of X. fastidiosa NAGS/K without his-tag
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
C | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
D | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
E | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
F | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
G | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
H | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NLG A 501 |
Chain | Residue |
A | PHE315 |
A | HOH608 |
A | HOH609 |
A | HOH631 |
A | HOH660 |
A | HOH726 |
A | HOH819 |
A | HOH832 |
A | TYR352 |
A | LEU353 |
A | ASP354 |
A | LYS355 |
A | PHE356 |
A | ARG385 |
A | ARG387 |
A | HOH605 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 502 |
Chain | Residue |
A | SER314 |
A | PHE356 |
A | ALA357 |
A | VAL358 |
A | ASN390 |
A | GLN391 |
A | HOH668 |
A | HOH772 |
A | HOH774 |
A | HOH778 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 503 |
Chain | Residue |
A | GLY366 |
A | LEU367 |
A | GLY368 |
A | ARG369 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE NLG B 600 |
Chain | Residue |
B | PHE315 |
B | TYR352 |
B | LEU353 |
B | ASP354 |
B | LYS355 |
B | PHE356 |
B | ARG385 |
B | SER386 |
B | ARG387 |
B | ASN390 |
B | TYR396 |
B | HOH701 |
B | HOH702 |
B | HOH704 |
B | HOH708 |
B | HOH713 |
B | HOH723 |
B | HOH731 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NLG C 501 |
Chain | Residue |
C | PHE315 |
C | ARG317 |
C | TYR352 |
C | LEU353 |
C | ASP354 |
C | LYS355 |
C | PHE356 |
C | ARG385 |
C | ARG387 |
C | LEU436 |
C | HOH601 |
C | HOH606 |
C | HOH634 |
C | HOH687 |
C | HOH862 |
C | HOH864 |
E | HOH676 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL C 502 |
Chain | Residue |
C | GLY366 |
C | GLY368 |
C | ARG369 |
C | HOH621 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL C 503 |
Chain | Residue |
C | SER335 |
C | ASN337 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NLG D 501 |
Chain | Residue |
D | PHE315 |
D | LEU353 |
D | ASP354 |
D | LYS355 |
D | PHE356 |
D | ARG385 |
D | ARG387 |
D | ASN390 |
D | TYR396 |
D | HOH602 |
D | HOH603 |
D | HOH605 |
D | HOH609 |
D | HOH620 |
D | HOH726 |
D | HOH770 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL D 502 |
Chain | Residue |
D | ARG317 |
D | ARG387 |
site_id | BC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NLG E 501 |
Chain | Residue |
E | TRP409 |
E | HOH607 |
E | HOH621 |
E | HOH624 |
E | HOH629 |
E | HOH666 |
E | PHE315 |
E | ARG317 |
E | ASP354 |
E | LYS355 |
E | PHE356 |
E | ARG385 |
E | SER386 |
E | ARG387 |
E | ASN390 |
E | TYR396 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL E 502 |
Chain | Residue |
E | GLY366 |
E | GLY368 |
E | ARG369 |
E | HOH773 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL E 503 |
Chain | Residue |
E | SER335 |
E | ASN337 |
H | ASN389 |
site_id | BC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE NLG F 600 |
Chain | Residue |
F | PHE315 |
F | ARG317 |
F | TYR352 |
F | LEU353 |
F | ASP354 |
F | LYS355 |
F | PHE356 |
F | ARG385 |
F | ARG387 |
F | TRP409 |
F | HOH701 |
F | HOH702 |
F | HOH708 |
F | HOH712 |
F | HOH759 |
site_id | BC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE NLG G 501 |
Chain | Residue |
G | PHE315 |
G | ARG317 |
G | TYR352 |
G | LEU353 |
G | ASP354 |
G | LYS355 |
G | PHE356 |
G | ARG385 |
G | ARG387 |
G | HOH601 |
G | HOH602 |
G | HOH605 |
G | HOH625 |
G | HOH682 |
G | HOH773 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL G 502 |
Chain | Residue |
G | PHE356 |
G | GLY368 |
G | PHE395 |
G | CL503 |
G | HOH606 |
G | HOH751 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL G 503 |
Chain | Residue |
G | GLY366 |
G | LEU367 |
G | GLY368 |
G | ARG369 |
G | GOL502 |
G | HOH653 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL G 504 |
Chain | Residue |
G | SER335 |
G | ASN337 |
G | ARG339 |
G | HOH728 |
site_id | BC9 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE NLG H 600 |
Chain | Residue |
H | PHE315 |
H | TYR352 |
H | ASP354 |
H | LYS355 |
H | PHE356 |
H | ARG385 |
H | SER386 |
H | ARG387 |
H | ASN390 |
H | TYR396 |
H | HOH703 |
H | HOH705 |
H | HOH708 |
H | HOH714 |
H | HOH738 |
H | HOH754 |
H | HOH821 |