6C8Q
Crystal structure of NAD synthetase (NadE) from Enterococcus faecalis in complex with NAD+
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
A | 0004359 | molecular_function | glutaminase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0008795 | molecular_function | NAD+ synthase activity |
A | 0009435 | biological_process | NAD biosynthetic process |
A | 0016874 | molecular_function | ligase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
B | 0004359 | molecular_function | glutaminase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0008795 | molecular_function | NAD+ synthase activity |
B | 0009435 | biological_process | NAD biosynthetic process |
B | 0016874 | molecular_function | ligase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
C | 0004359 | molecular_function | glutaminase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0008795 | molecular_function | NAD+ synthase activity |
C | 0009435 | biological_process | NAD biosynthetic process |
C | 0016874 | molecular_function | ligase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
D | 0004359 | molecular_function | glutaminase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0008795 | molecular_function | NAD+ synthase activity |
D | 0009435 | biological_process | NAD biosynthetic process |
D | 0016874 | molecular_function | ligase activity |
D | 0046872 | molecular_function | metal ion binding |
E | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
E | 0004359 | molecular_function | glutaminase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0008795 | molecular_function | NAD+ synthase activity |
E | 0009435 | biological_process | NAD biosynthetic process |
E | 0016874 | molecular_function | ligase activity |
E | 0046872 | molecular_function | metal ion binding |
F | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
F | 0004359 | molecular_function | glutaminase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0008795 | molecular_function | NAD+ synthase activity |
F | 0009435 | biological_process | NAD biosynthetic process |
F | 0016874 | molecular_function | ligase activity |
F | 0046872 | molecular_function | metal ion binding |
G | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
G | 0004359 | molecular_function | glutaminase activity |
G | 0005524 | molecular_function | ATP binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0008795 | molecular_function | NAD+ synthase activity |
G | 0009435 | biological_process | NAD biosynthetic process |
G | 0016874 | molecular_function | ligase activity |
G | 0046872 | molecular_function | metal ion binding |
H | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
H | 0004359 | molecular_function | glutaminase activity |
H | 0005524 | molecular_function | ATP binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0008795 | molecular_function | NAD+ synthase activity |
H | 0009435 | biological_process | NAD biosynthetic process |
H | 0016874 | molecular_function | ligase activity |
H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue NAD A 301 |
Chain | Residue |
A | PHE133 |
A | LYS262 |
A | HOH402 |
A | HOH455 |
A | HOH490 |
B | TYR34 |
B | HIS38 |
B | PHE40 |
B | TYR148 |
B | GLY156 |
B | ASP181 |
A | ASN137 |
C | VAL226 |
C | GLY229 |
A | ARG141 |
A | PHE171 |
A | PHE172 |
A | THR173 |
A | LYS174 |
A | ALA227 |
A | HIS261 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue NAD B 301 |
Chain | Residue |
A | TYR34 |
A | HIS38 |
A | PHE40 |
A | TYR148 |
A | GLY156 |
A | ASP181 |
B | PHE133 |
B | ASN137 |
B | ARG141 |
B | ALA170 |
B | PHE171 |
B | PHE172 |
B | THR173 |
B | LYS174 |
B | ALA227 |
B | HIS261 |
B | LYS262 |
B | HOH472 |
site_id | AC3 |
Number of Residues | 21 |
Details | binding site for residue NAD C 301 |
Chain | Residue |
A | VAL226 |
A | GLY229 |
C | PHE133 |
C | ASN137 |
C | ARG141 |
C | ALA170 |
C | PHE171 |
C | PHE172 |
C | THR173 |
C | LYS174 |
C | ALA227 |
C | HIS261 |
C | LYS262 |
C | HOH401 |
C | HOH411 |
G | TYR34 |
G | HIS38 |
G | PHE40 |
G | TYR148 |
G | GLY156 |
G | ASP181 |
site_id | AC4 |
Number of Residues | 15 |
Details | binding site for residue NAD D 301 |
Chain | Residue |
D | PHE133 |
D | ASN137 |
D | ARG141 |
D | PHE171 |
D | PHE172 |
D | LYS174 |
D | HIS261 |
D | LYS262 |
D | HOH419 |
D | HOH462 |
F | TYR34 |
F | HIS38 |
F | PHE40 |
F | GLY156 |
F | ASP181 |
site_id | AC5 |
Number of Residues | 16 |
Details | binding site for residue NAD E 301 |
Chain | Residue |
E | PHE133 |
E | ASN137 |
E | ARG141 |
E | PHE171 |
E | PHE172 |
E | THR173 |
E | LYS174 |
E | HIS261 |
E | LYS262 |
E | HOH415 |
H | TYR34 |
H | HIS38 |
H | PHE40 |
H | GLY156 |
H | ALA157 |
H | ASP181 |
site_id | AC6 |
Number of Residues | 16 |
Details | binding site for residue NAD F 301 |
Chain | Residue |
F | ASN137 |
F | ARG141 |
F | PHE171 |
F | PHE172 |
F | THR173 |
F | LYS174 |
F | HIS261 |
F | LYS262 |
D | TYR34 |
D | HIS38 |
D | LEU41 |
D | TYR148 |
D | GLY156 |
D | ASP181 |
F | PHE133 |
F | GLY136 |
site_id | AC7 |
Number of Residues | 20 |
Details | binding site for residue NAD G 301 |
Chain | Residue |
C | TYR34 |
C | HIS38 |
C | PHE40 |
C | TYR148 |
C | GLY156 |
C | ASP181 |
G | PHE133 |
G | ASN137 |
G | ARG141 |
G | GLU166 |
G | PHE171 |
G | PHE172 |
G | THR173 |
G | LYS174 |
G | ASP177 |
G | ASP224 |
G | HIS261 |
G | LYS262 |
G | HOH407 |
G | HOH457 |
site_id | AC8 |
Number of Residues | 17 |
Details | binding site for residue NAD H 301 |
Chain | Residue |
E | TYR34 |
E | HIS38 |
E | PHE40 |
E | TYR148 |
E | GLY156 |
E | ASP181 |
H | PHE133 |
H | ASN137 |
H | ARG141 |
H | PHE171 |
H | PHE172 |
H | THR173 |
H | LYS174 |
H | HIS261 |
H | LYS262 |
H | HOH435 |
H | HOH459 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 80 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193 |
Chain | Residue | Details |
A | THR212 | |
A | HIS261 | |
B | GLY47 | |
B | ASP53 | |
B | ARG141 | |
B | THR161 | |
B | GLU166 | |
B | LYS174 | |
B | ASP181 | |
B | LYS190 | |
B | THR212 | |
B | HIS261 | |
C | GLY47 | |
C | ASP53 | |
C | ARG141 | |
C | THR161 | |
C | GLU166 | |
C | LYS174 | |
C | ASP181 | |
C | LYS190 | |
C | THR212 | |
C | HIS261 | |
D | GLY47 | |
D | ASP53 | |
D | ARG141 | |
D | THR161 | |
D | GLU166 | |
D | LYS174 | |
D | ASP181 | |
D | LYS190 | |
D | THR212 | |
D | HIS261 | |
E | GLY47 | |
E | ASP53 | |
E | ARG141 | |
E | THR161 | |
E | GLU166 | |
E | LYS174 | |
E | ASP181 | |
E | LYS190 | |
E | THR212 | |
E | HIS261 | |
F | GLY47 | |
F | ASP53 | |
F | ARG141 | |
F | THR161 | |
F | GLU166 | |
F | LYS174 | |
F | ASP181 | |
F | LYS190 | |
F | THR212 | |
F | HIS261 | |
G | GLY47 | |
G | ASP53 | |
G | ARG141 | |
G | THR161 | |
G | GLU166 | |
G | LYS174 | |
G | ASP181 | |
G | LYS190 | |
G | THR212 | |
G | HIS261 | |
H | GLY47 | |
H | ASP53 | |
H | ARG141 | |
H | THR161 | |
H | GLU166 | |
H | LYS174 | |
H | ASP181 | |
H | LYS190 | |
H | THR212 | |
H | HIS261 | |
A | GLY47 | |
A | ASP53 | |
A | ARG141 | |
A | THR161 | |
A | GLU166 | |
A | LYS174 | |
A | ASP181 | |
A | LYS190 |