6OAY
Structure of the hyperactive ClpB mutant K476C, bound to casein, post-state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009408 | biological_process | response to heat |
A | 0016020 | cellular_component | membrane |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0034605 | biological_process | cellular response to heat |
A | 0042026 | biological_process | protein refolding |
A | 0042802 | molecular_function | identical protein binding |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0009408 | biological_process | response to heat |
B | 0016020 | cellular_component | membrane |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0034605 | biological_process | cellular response to heat |
B | 0042026 | biological_process | protein refolding |
B | 0042802 | molecular_function | identical protein binding |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0009408 | biological_process | response to heat |
C | 0016020 | cellular_component | membrane |
C | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0034605 | biological_process | cellular response to heat |
C | 0042026 | biological_process | protein refolding |
C | 0042802 | molecular_function | identical protein binding |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0009408 | biological_process | response to heat |
D | 0016020 | cellular_component | membrane |
D | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0034605 | biological_process | cellular response to heat |
D | 0042026 | biological_process | protein refolding |
D | 0042802 | molecular_function | identical protein binding |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0009408 | biological_process | response to heat |
E | 0016020 | cellular_component | membrane |
E | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0034605 | biological_process | cellular response to heat |
E | 0042026 | biological_process | protein refolding |
E | 0042802 | molecular_function | identical protein binding |
F | 0005515 | molecular_function | protein binding |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0009408 | biological_process | response to heat |
F | 0016020 | cellular_component | membrane |
F | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0034605 | biological_process | cellular response to heat |
F | 0042026 | biological_process | protein refolding |
F | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue AGS C 901 |
Chain | Residue |
B | ARG332 |
C | THR213 |
C | ALA214 |
C | GLU279 |
C | ILE349 |
C | LEU353 |
C | PRO179 |
C | VAL180 |
C | ILE181 |
C | ARG183 |
C | PRO208 |
C | GLY209 |
C | GLY211 |
C | LYS212 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue AGS C 902 |
Chain | Residue |
C | ARG569 |
C | VAL570 |
C | ILE571 |
C | PRO606 |
C | THR607 |
C | GLY608 |
C | VAL609 |
C | GLY610 |
C | LYS611 |
C | THR612 |
C | GLU613 |
C | GLU678 |
C | ASN719 |
C | ILE774 |
C | ILE777 |
C | GLN778 |
C | ARG815 |
C | LYS818 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue ADP F 901 |
Chain | Residue |
E | ARG331 |
F | ASP178 |
F | GLY209 |
F | VAL210 |
F | GLY211 |
F | LYS212 |
F | THR213 |
F | GLU217 |
F | ILE349 |
F | LEU350 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue AGS E 901 |
Chain | Residue |
D | ARG331 |
D | ARG332 |
E | VAL180 |
E | ILE181 |
E | ARG183 |
E | GLY209 |
E | VAL210 |
E | GLY211 |
E | LYS212 |
E | THR213 |
E | ALA214 |
E | ASP278 |
E | ILE349 |
E | LEU353 |
E | ASP388 |
E | ILE391 |
site_id | AC5 |
Number of Residues | 16 |
Details | binding site for residue AGS E 902 |
Chain | Residue |
D | GLU752 |
D | ARG756 |
E | ARG569 |
E | VAL570 |
E | ILE571 |
E | GLY608 |
E | VAL609 |
E | GLY610 |
E | LYS611 |
E | THR612 |
E | GLU613 |
E | ASN719 |
E | ILE774 |
E | GLN778 |
E | ARG815 |
E | LYS818 |
site_id | AC6 |
Number of Residues | 15 |
Details | binding site for residue AGS D 901 |
Chain | Residue |
C | ARG332 |
D | PRO179 |
D | VAL180 |
D | ILE181 |
D | GLY209 |
D | VAL210 |
D | GLY211 |
D | LYS212 |
D | THR213 |
D | ALA214 |
D | THR315 |
D | ILE349 |
D | LEU353 |
D | ASP388 |
D | ILE391 |
site_id | AC7 |
Number of Residues | 18 |
Details | binding site for residue AGS D 902 |
Chain | Residue |
D | THR612 |
D | GLU613 |
D | GLU678 |
D | ILE774 |
D | GLN778 |
D | ALA814 |
D | ARG815 |
D | LYS818 |
C | ARG756 |
D | ARG569 |
D | VAL570 |
D | ILE571 |
D | GLN573 |
D | THR607 |
D | GLY608 |
D | VAL609 |
D | GLY610 |
D | LYS611 |
site_id | AC8 |
Number of Residues | 16 |
Details | binding site for residue AGS B 901 |
Chain | Residue |
A | ALA327 |
A | ARG331 |
B | ASP178 |
B | PRO179 |
B | VAL180 |
B | ILE181 |
B | ARG183 |
B | PRO208 |
B | GLY209 |
B | VAL210 |
B | GLY211 |
B | LYS212 |
B | THR213 |
B | ALA214 |
B | LEU353 |
B | ILE391 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue ADP B 902 |
Chain | Residue |
B | ARG569 |
B | VAL570 |
B | THR607 |
B | GLY608 |
B | VAL609 |
B | GLY610 |
B | LYS611 |
B | THR612 |
B | GLU613 |
B | LEU766 |
B | ILE774 |
B | ALA814 |
site_id | AD1 |
Number of Residues | 12 |
Details | binding site for residue ADP A 901 |
Chain | Residue |
A | ASP178 |
A | PRO179 |
A | VAL180 |
A | ILE181 |
A | GLY209 |
A | VAL210 |
A | GLY211 |
A | LYS212 |
A | THR213 |
A | ALA214 |
A | ILE349 |
F | ARG331 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue ADP A 902 |
Chain | Residue |
A | THR607 |
A | GLY608 |
A | THR612 |
A | GLU613 |
A | ILE774 |
F | ASN595 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
D | GLY206 | |
D | GLY605 | |
B | GLY206 | |
B | GLY605 | |
A | GLY206 | |
A | GLY605 | |
C | GLY206 | |
C | GLY605 | |
F | GLY206 | |
F | GLY605 | |
E | GLY206 | |
E | GLY605 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
E | ASN96 | |
E | LYS176 | |
E | LYS640 | |
D | ASN96 | |
D | LYS176 | |
D | LYS640 | |
B | ASN96 | |
B | LYS176 | |
B | LYS640 | |
A | ASN96 | |
A | LYS176 | |
A | LYS640 | |
C | ASN96 | |
C | LYS176 | |
C | LYS640 | |
F | ASN96 | |
F | LYS176 | |
F | LYS640 |