5EJF
Crystal structure of NAD kinase P101A mutant from Listeria monocytogenes
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003951 | molecular_function | NAD+ kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006741 | biological_process | NADP biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0019674 | biological_process | NAD metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0051287 | molecular_function | NAD binding |
B | 0003951 | molecular_function | NAD+ kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006741 | biological_process | NADP biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0019674 | biological_process | NAD metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0051287 | molecular_function | NAD binding |
C | 0003951 | molecular_function | NAD+ kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006741 | biological_process | NADP biosynthetic process |
C | 0016301 | molecular_function | kinase activity |
C | 0016310 | biological_process | phosphorylation |
C | 0019674 | biological_process | NAD metabolic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0051287 | molecular_function | NAD binding |
D | 0003951 | molecular_function | NAD+ kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006741 | biological_process | NADP biosynthetic process |
D | 0016301 | molecular_function | kinase activity |
D | 0016310 | biological_process | phosphorylation |
D | 0019674 | biological_process | NAD metabolic process |
D | 0046872 | molecular_function | metal ion binding |
D | 0051287 | molecular_function | NAD binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780 |
Chain | Residue | Details |
A | ASP45 | |
B | ASP45 | |
C | ASP45 | |
D | ASP45 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780 |
Chain | Residue | Details |
A | ASP45 | |
B | SER158 | |
B | THR161 | |
B | HIS223 | |
C | ASP45 | |
C | GLY46 | |
C | ASN122 | |
C | SER158 | |
C | THR161 | |
C | HIS223 | |
D | ASP45 | |
A | GLY46 | |
D | GLY46 | |
D | ASN122 | |
D | SER158 | |
D | THR161 | |
D | HIS223 | |
A | ASN122 | |
A | SER158 | |
A | THR161 | |
A | HIS223 | |
B | ASP45 | |
B | GLY46 | |
B | ASN122 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00361 |
Chain | Residue | Details |
A | ARG148 | |
B | ARG148 | |
C | ARG148 | |
D | ARG148 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:17686780 |
Chain | Residue | Details |
A | ASP150 | |
B | ASP150 | |
C | ASP150 | |
D | ASP150 |