5O5O
X-ray crystal structure of RapZ from Escherichia coli (P32 space group)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0050779 | biological_process | RNA destabilization |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0060090 | molecular_function | molecular adaptor activity |
| A | 0097367 | molecular_function | carbohydrate derivative binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0050779 | biological_process | RNA destabilization |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0060090 | molecular_function | molecular adaptor activity |
| B | 0097367 | molecular_function | carbohydrate derivative binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003723 | molecular_function | RNA binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005525 | molecular_function | GTP binding |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0050779 | biological_process | RNA destabilization |
| C | 0051289 | biological_process | protein homotetramerization |
| C | 0060090 | molecular_function | molecular adaptor activity |
| C | 0097367 | molecular_function | carbohydrate derivative binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003723 | molecular_function | RNA binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005525 | molecular_function | GTP binding |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0050779 | biological_process | RNA destabilization |
| D | 0051289 | biological_process | protein homotetramerization |
| D | 0060090 | molecular_function | molecular adaptor activity |
| D | 0097367 | molecular_function | carbohydrate derivative binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | ASN188 |
| A | HIS190 |
| A | CYS247 |
| A | THR248 |
| A | GLY249 |
| A | ARG253 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | GLY13 |
| A | LYS14 |
| A | SER15 |
| A | SER10 |
| A | GLY11 |
| A | SER12 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 301 |
| Chain | Residue |
| B | ASN188 |
| B | HIS190 |
| B | CYS247 |
| B | THR248 |
| B | GLY249 |
| B | ARG253 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| B | ASN188 |
| B | ARG253 |
| C | THR150 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 301 |
| Chain | Residue |
| A | THR235 |
| C | HIS190 |
| C | CYS247 |
| C | THR248 |
| C | GLY249 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 302 |
| Chain | Residue |
| A | TYR220 |
| A | ARG223 |
| C | ARG101 |
| C | LEU102 |
| C | HIS103 |
| C | ASN109 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 D 301 |
| Chain | Residue |
| B | THR235 |
| D | HIS190 |
| D | CYS247 |
| D | THR248 |
| D | GLY249 |
| D | GLY250 |
| D | LYS251 |
| D | HIS252 |
| D | ARG253 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 302 |
| Chain | Residue |
| B | TYR220 |
| B | ARG223 |
| D | ARG101 |
| D | LEU102 |
| D | HIS103 |
| D | ASN109 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 303 |
| Chain | Residue |
| D | ARG95 |
| D | MET139 |
| D | SER140 |
| D | VAL141 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 D 304 |
| Chain | Residue |
| D | GLY11 |
| D | SER12 |
| D | GLY13 |
| D | LYS14 |
| D | SER15 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide SO4 B 303 and LYS B 14 |
| Chain | Residue |
| B | SER7 |
| B | GLY8 |
| B | GLY11 |
| B | GLY13 |
| B | SER15 |
| B | VAL16 |
| B | ALA17 |
| B | LEU18 |
| B | ASP56 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide SO4 C 303 and LYS C 14 |
| Chain | Residue |
| C | VAL6 |
| C | GLY8 |
| C | ARG9 |
| C | SER10 |
| C | GLY11 |
| C | SER12 |
| C | GLY13 |
| C | SER15 |
| C | VAL16 |
| C | ALA17 |
| C | LEU18 |
| C | ASP56 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00636 |
| Chain | Residue | Details |
| C | GLY8 | |
| C | ASP56 | |
| D | GLY8 | |
| D | ASP56 | |
| A | GLY8 | |
| A | ASP56 | |
| B | GLY8 | |
| B | ASP56 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS251 | |
| B | LYS251 | |
| C | LYS251 | |
| D | LYS251 |
