Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0004386 | molecular_function | helicase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006310 | biological_process | DNA recombination |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0004386 | molecular_function | helicase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006310 | biological_process | DNA recombination |
C | 0003676 | molecular_function | nucleic acid binding |
C | 0004386 | molecular_function | helicase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006310 | biological_process | DNA recombination |
D | 0003676 | molecular_function | nucleic acid binding |
D | 0004386 | molecular_function | helicase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006310 | biological_process | DNA recombination |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 501 |
Chain | Residue |
A | CYS411 |
A | CYS427 |
A | CYS431 |
A | CYS434 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue DMS A 502 |
Chain | Residue |
A | ALA193 |
A | ALA195 |
A | TYR344 |
A | PHE420 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MG A 503 |
Chain | Residue |
A | HOH637 |
A | HOH672 |
A | HOH675 |
A | HOH691 |
A | ADP504 |
site_id | AC4 |
Number of Residues | 18 |
Details | binding site for residue ADP A 504 |
Chain | Residue |
A | PHE26 |
A | SER28 |
A | PHE29 |
A | LYS30 |
A | GLN34 |
A | PRO53 |
A | THR54 |
A | GLY55 |
A | ALA56 |
A | GLY57 |
A | LYS58 |
A | SER59 |
A | MG503 |
A | HOH610 |
A | HOH629 |
A | HOH637 |
A | HOH663 |
A | HOH675 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | CYS411 |
B | CYS427 |
B | CYS431 |
B | CYS434 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue DMS B 502 |
Chain | Residue |
B | TYR265 |
B | ILE317 |
B | SER318 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue MG B 503 |
Chain | Residue |
B | ADP504 |
B | HOH605 |
B | HOH630 |
B | HOH684 |
B | HOH686 |
site_id | AC8 |
Number of Residues | 18 |
Details | binding site for residue ADP B 504 |
Chain | Residue |
B | PHE26 |
B | SER28 |
B | PHE29 |
B | LYS30 |
B | GLN34 |
B | PRO53 |
B | THR54 |
B | GLY55 |
B | ALA56 |
B | GLY57 |
B | LYS58 |
B | SER59 |
B | MG503 |
B | HOH610 |
B | HOH613 |
B | HOH630 |
B | HOH674 |
B | HOH684 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue ZN C 501 |
Chain | Residue |
C | CYS411 |
C | CYS427 |
C | CYS431 |
C | CYS434 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue MG C 502 |
Chain | Residue |
C | ADP503 |
C | HOH615 |
C | HOH657 |
C | HOH668 |
site_id | AD2 |
Number of Residues | 15 |
Details | binding site for residue ADP C 503 |
Chain | Residue |
C | PHE26 |
C | SER28 |
C | LYS30 |
C | GLN34 |
C | PRO53 |
C | THR54 |
C | GLY55 |
C | ALA56 |
C | GLY57 |
C | LYS58 |
C | SER59 |
C | MG502 |
C | HOH615 |
C | HOH653 |
C | HOH657 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue ZN D 501 |
Chain | Residue |
D | CYS411 |
D | CYS427 |
D | CYS431 |
D | CYS434 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue DMS D 502 |
Chain | Residue |
D | TYR265 |
D | SER318 |
D | PHE319 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue MG D 503 |
Chain | Residue |
D | ADP504 |
D | HOH610 |
D | HOH618 |
D | HOH649 |
D | HOH660 |
site_id | AD6 |
Number of Residues | 13 |
Details | binding site for residue ADP D 504 |
Chain | Residue |
D | GLN34 |
D | PRO53 |
D | GLY55 |
D | ALA56 |
D | GLY57 |
D | LYS58 |
D | SER59 |
D | MG503 |
D | HOH610 |
D | HOH618 |
D | PHE26 |
D | SER28 |
D | LYS30 |
Functional Information from PROSITE/UniProt
site_id | PS00690 |
Number of Residues | 10 |
Details | DEAH_ATP_HELICASE DEAH-box subfamily ATP-dependent helicases signature. SyLVVDEAHC |
Chain | Residue | Details |
A | SER152-CYS161 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | PHE26 | |
B | PHE26 | |
B | SER28 | |
B | LYS30 | |
B | GLN34 | |
B | GLY55 | |
B | ALA56 | |
B | GLY57 | |
B | LYS58 | |
B | SER59 | |
C | PHE26 | |
A | SER28 | |
C | SER28 | |
C | LYS30 | |
C | GLN34 | |
C | GLY55 | |
C | ALA56 | |
C | GLY57 | |
C | LYS58 | |
C | SER59 | |
D | PHE26 | |
D | SER28 | |
A | LYS30 | |
D | LYS30 | |
D | GLN34 | |
D | GLY55 | |
D | ALA56 | |
D | GLY57 | |
D | LYS58 | |
D | SER59 | |
A | GLN34 | |
A | GLY55 | |
A | ALA56 | |
A | GLY57 | |
A | LYS58 | |
A | SER59 | |
Chain | Residue | Details |
A | PRO53 | |
B | PRO53 | |
C | PRO53 | |
D | PRO53 | |
Chain | Residue | Details |
A | CYS411 | |
D | CYS411 | |
D | CYS431 | |
D | CYS434 | |
A | CYS431 | |
A | CYS434 | |
B | CYS411 | |
B | CYS431 | |
B | CYS434 | |
C | CYS411 | |
C | CYS431 | |
C | CYS434 | |
Chain | Residue | Details |
A | CYS427 | |
B | CYS427 | |
C | CYS427 | |
D | CYS427 | |