3LF0
Crystal structure of the ATP bound Mycobacterium tuberculosis nitrogen regulatory PII protein
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006808 | biological_process | regulation of nitrogen utilization |
A | 0030234 | molecular_function | enzyme regulator activity |
A | 0043531 | molecular_function | ADP binding |
A | 0051701 | biological_process | biological process involved in interaction with host |
B | 0000166 | molecular_function | nucleotide binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006808 | biological_process | regulation of nitrogen utilization |
B | 0030234 | molecular_function | enzyme regulator activity |
B | 0043531 | molecular_function | ADP binding |
B | 0051701 | biological_process | biological process involved in interaction with host |
C | 0000166 | molecular_function | nucleotide binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006808 | biological_process | regulation of nitrogen utilization |
C | 0030234 | molecular_function | enzyme regulator activity |
C | 0043531 | molecular_function | ADP binding |
C | 0051701 | biological_process | biological process involved in interaction with host |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE ATP A 701 |
Chain | Residue |
A | ILE7 |
A | LYS90 |
A | HOH128 |
A | HOH148 |
B | GLY27 |
B | MET28 |
B | THR29 |
B | GLU62 |
B | VAL63 |
B | VAL64 |
B | ARG101 |
A | GLY35 |
B | ARG103 |
B | HOH143 |
A | TYR36 |
A | GLY37 |
A | ARG38 |
A | ILE86 |
A | GLY87 |
A | ASP88 |
A | GLY89 |
site_id | AC2 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE ATP B 701 |
Chain | Residue |
B | ILE7 |
B | ILE33 |
B | GLY35 |
B | TYR36 |
B | GLY37 |
B | ARG38 |
B | GLN39 |
B | LYS58 |
B | ILE86 |
B | GLY87 |
B | ASP88 |
B | GLY89 |
B | LYS90 |
B | HOH134 |
B | HOH144 |
C | GLY27 |
C | MET28 |
C | THR29 |
C | GLU62 |
C | VAL63 |
C | VAL64 |
C | ARG101 |
C | ARG103 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ATP C 701 |
Chain | Residue |
A | GLY27 |
A | MET28 |
A | VAL63 |
A | VAL64 |
A | ARG101 |
A | ARG103 |
C | ILE7 |
C | GLY35 |
C | TYR36 |
C | GLY37 |
C | ARG38 |
C | LYS58 |
C | ILE86 |
C | GLY87 |
C | ASP88 |
C | GLY89 |
C | LYS90 |
C | HOH130 |
C | HOH139 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | MOD_RES: O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 |
Chain | Residue | Details |
A | TYR51 | |
B | TYR51 | |
C | TYR51 |