3V6I
Crystal structure of the peripheral stalk of Thermus thermophilus H+-ATPase/synthase at 2.25 A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0006754 | biological_process | ATP biosynthetic process |
A | 0033178 | cellular_component | proton-transporting two-sector ATPase complex, catalytic domain |
A | 0042777 | biological_process | proton motive force-driven plasma membrane ATP synthesis |
A | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
A | 0046961 | molecular_function | proton-transporting ATPase activity, rotational mechanism |
A | 1902600 | biological_process | proton transmembrane transport |
Y | 0005515 | molecular_function | protein binding |
Y | 0005524 | molecular_function | ATP binding |
Y | 0006754 | biological_process | ATP biosynthetic process |
Y | 0033178 | cellular_component | proton-transporting two-sector ATPase complex, catalytic domain |
Y | 0042777 | biological_process | proton motive force-driven plasma membrane ATP synthesis |
Y | 0046933 | molecular_function | proton-transporting ATP synthase activity, rotational mechanism |
Y | 0046961 | molecular_function | proton-transporting ATPase activity, rotational mechanism |
Y | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 201 |
Chain | Residue |
A | GLU13 |
A | GLN17 |
A | CA204 |
A | HOH334 |
A | HOH336 |
B | ASP108 |
B | HOH308 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 202 |
Chain | Residue |
A | HOH335 |
B | ALA105 |
B | HOH308 |
A | GLU13 |
A | CA204 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 203 |
Chain | Residue |
A | GLU22 |
A | GLU113 |
A | HOH319 |
A | HOH330 |
A | HOH340 |
Y | HOH305 |
Y | HOH307 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 204 |
Chain | Residue |
A | GLN10 |
A | CA201 |
A | CA202 |
B | ALA105 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA B 201 |
Chain | Residue |
B | GLU117 |
Y | GLU61 |
Y | HOH304 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA X 201 |
Chain | Residue |
A | HOH309 |
X | GLU117 |
X | HOH313 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA X 202 |
Chain | Residue |
X | GLU38 |
X | GLU90 |
X | GLU93 |
X | HOH315 |
X | HOH316 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA Y 201 |
Chain | Residue |
A | HOH333 |
Y | GLU22 |
Y | GLU113 |
Y | HOH312 |
Y | HOH317 |