7US2
PARL-cleaved Skd3 (human ClpB) E455Q Nucleotide Binding Domain hexamer bound to ATPgammaS, open conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0005524 | molecular_function | ATP binding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0005524 | molecular_function | ATP binding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0005524 | molecular_function | ATP binding |
D | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0005524 | molecular_function | ATP binding |
E | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0005524 | molecular_function | ATP binding |
F | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:36170828, ECO:0007744|PDB:7TTR, ECO:0007744|PDB:7TTS |
Chain | Residue | Details |
A | HIS346 | |
E | GLY384 | |
F | HIS346 | |
F | GLY384 | |
A | GLY384 | |
B | HIS346 | |
B | GLY384 | |
C | HIS346 | |
C | GLY384 | |
D | HIS346 | |
D | GLY384 | |
E | HIS346 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:36170828, ECO:0000269|PubMed:36745679, ECO:0007744|PDB:7TTR, ECO:0007744|PDB:7TTS, ECO:0007744|PDB:7XBK |
Chain | Residue | Details |
A | ILE348 | |
C | GLY386 | |
C | THR388 | |
C | ARG620 | |
D | ILE348 | |
D | GLY386 | |
D | THR388 | |
D | ARG620 | |
E | ILE348 | |
E | GLY386 | |
E | THR388 | |
A | GLY386 | |
E | ARG620 | |
F | ILE348 | |
F | GLY386 | |
F | THR388 | |
F | ARG620 | |
A | THR388 | |
A | ARG620 | |
B | ILE348 | |
B | GLY386 | |
B | THR388 | |
B | ARG620 | |
C | ILE348 |
site_id | SWS_FT_FI3 |
Number of Residues | 36 |
Details | BINDING: BINDING => ECO:0000269|PubMed:36745679, ECO:0007744|PDB:7XBK |
Chain | Residue | Details |
A | SER383 | |
B | GLN455 | |
B | ASN496 | |
B | ARG561 | |
C | SER383 | |
C | ILE385 | |
C | LYS387 | |
C | GLN455 | |
C | ASN496 | |
C | ARG561 | |
D | SER383 | |
A | ILE385 | |
D | ILE385 | |
D | LYS387 | |
D | GLN455 | |
D | ASN496 | |
D | ARG561 | |
E | SER383 | |
E | ILE385 | |
E | LYS387 | |
E | GLN455 | |
E | ASN496 | |
A | LYS387 | |
E | ARG561 | |
F | SER383 | |
F | ILE385 | |
F | LYS387 | |
F | GLN455 | |
F | ASN496 | |
F | ARG561 | |
A | GLN455 | |
A | ASN496 | |
A | ARG561 | |
B | SER383 | |
B | ILE385 | |
B | LYS387 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS589 | |
B | LYS589 | |
C | LYS589 | |
D | LYS589 | |
E | LYS589 | |
F | LYS589 |