5O5Q
X-ray crystal structure of RapZ from Escherichia coli (P3221 space group)
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 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 | 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 | ARG9 |
A | GLY11 |
A | SER12 |
A | GLY13 |
A | LYS14 |
A | SER15 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 302 |
Chain | Residue |
A | GLY249 |
A | HIS252 |
A | ARG253 |
A | SO4304 |
A | ASN188 |
A | CYS247 |
A | THR248 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 303 |
Chain | Residue |
A | ARG184 |
A | ASN188 |
A | ARG253 |
B | ARG151 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 304 |
Chain | Residue |
A | HIS190 |
A | ARG196 |
A | HIS252 |
A | SO4302 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
B | ARG9 |
B | SER10 |
B | GLY11 |
B | SER12 |
B | GLY13 |
B | LYS14 |
B | SER15 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 302 |
Chain | Residue |
B | ARG101 |
B | LEU102 |
B | HIS103 |
B | ASN109 |
C | TYR220 |
C | ARG223 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue SO4 B 303 |
Chain | Residue |
B | ASN188 |
B | HIS190 |
B | CYS247 |
B | THR248 |
B | GLY249 |
B | HIS252 |
B | ARG253 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue SO4 D 301 |
Chain | Residue |
A | TYR220 |
A | ARG223 |
D | ARG101 |
D | LEU102 |
D | HIS103 |
D | ASN109 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue SO4 D 302 |
Chain | Residue |
D | ARG9 |
D | SER10 |
D | GLY11 |
D | SER12 |
D | GLY13 |
D | LYS14 |
D | SER15 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue SO4 D 303 |
Chain | Residue |
D | GLY11 |
D | ARG95 |
D | VAL141 |
D | SO4306 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue SO4 D 304 |
Chain | Residue |
D | SER97 |
D | ARG100 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue SO4 D 306 |
Chain | Residue |
D | SO4303 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 301 |
Chain | Residue |
C | ASN188 |
C | HIS190 |
C | THR248 |
C | GLY249 |
C | ARG253 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for Di-peptide SO4 C 302 and LYS C 14 |
Chain | Residue |
C | ARG9 |
C | GLY11 |
C | SER12 |
C | GLY13 |
C | SER15 |
C | VAL16 |
C | ALA17 |
C | LEU18 |
site_id | AD6 |
Number of Residues | 11 |
Details | binding site for Di-peptide SO4 D 305 and ARG D 253 |
Chain | Residue |
D | ARG184 |
D | PRO187 |
D | ASN188 |
D | CYS247 |
D | THR248 |
D | GLY249 |
D | HIS252 |
D | SER254 |
D | VAL255 |
D | TYR256 |
D | ILE257 |
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 |
A | GLY8 | |
A | ASP56 | |
B | GLY8 | |
B | ASP56 | |
D | GLY8 | |
D | ASP56 | |
C | GLY8 | |
C | 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 | |
D | LYS251 | |
C | LYS251 |