6R4Q
Crystal structure of the periplasmic nickel-binding protein NikA from Escherichia coli in complex with Ru(bpza)CO H2O Cl
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0015675 | biological_process | nickel cation transport |
A | 0015833 | biological_process | peptide transport |
A | 0016020 | cellular_component | membrane |
A | 0016151 | molecular_function | nickel cation binding |
A | 0020037 | molecular_function | heme binding |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0042597 | cellular_component | periplasmic space |
A | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
A | 0046914 | molecular_function | transition metal ion binding |
A | 0050919 | biological_process | negative chemotaxis |
A | 0051540 | molecular_function | metal cluster binding |
A | 0055052 | cellular_component | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing |
A | 0055085 | biological_process | transmembrane transport |
A | 0098716 | biological_process | nickel cation import across plasma membrane |
A | 1904680 | molecular_function | peptide transmembrane transporter activity |
B | 0005515 | molecular_function | protein binding |
B | 0015675 | biological_process | nickel cation transport |
B | 0015833 | biological_process | peptide transport |
B | 0016020 | cellular_component | membrane |
B | 0016151 | molecular_function | nickel cation binding |
B | 0020037 | molecular_function | heme binding |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0042597 | cellular_component | periplasmic space |
B | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
B | 0046914 | molecular_function | transition metal ion binding |
B | 0050919 | biological_process | negative chemotaxis |
B | 0051540 | molecular_function | metal cluster binding |
B | 0055052 | cellular_component | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing |
B | 0055085 | biological_process | transmembrane transport |
B | 0098716 | biological_process | nickel cation import across plasma membrane |
B | 1904680 | molecular_function | peptide transmembrane transporter activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue FE A 601 |
Chain | Residue |
A | EDT602 |
A | HOH701 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue EDT A 602 |
Chain | Residue |
A | FE601 |
A | HOH701 |
A | HOH766 |
A | HOH865 |
A | HOH911 |
A | TYR22 |
A | MET27 |
A | ARG97 |
A | TRP100 |
A | ARG137 |
A | TRP398 |
A | THR490 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CL A 603 |
Chain | Residue |
A | GLU221 |
A | GLY222 |
A | LEU224 |
A | LEU226 |
A | HOH985 |
A | HOH1055 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 604 |
Chain | Residue |
A | LEU305 |
A | LYS306 |
A | THR456 |
A | ASP460 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue GOL A 605 |
Chain | Residue |
A | GLN361 |
A | ASP370 |
A | SER372 |
A | LEU373 |
A | HOH846 |
B | LYS157 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue GOL A 606 |
Chain | Residue |
A | GLN41 |
A | ALA42 |
A | ASP43 |
A | HOH852 |
A | HOH867 |
B | GLN41 |
B | ALA42 |
B | PRO487 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GOL A 607 |
Chain | Residue |
A | ARG95 |
A | VAL108 |
A | ASP109 |
A | VAL110 |
A | ASN281 |
A | HOH1008 |
A | HOH1012 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue GOL A 608 |
Chain | Residue |
A | ALA99 |
A | TRP100 |
A | GLU102 |
A | ASN105 |
A | SER409 |
A | SER410 |
A | ARG412 |
A | VAL413 |
A | GOL615 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue GOL A 609 |
Chain | Residue |
A | LYS257 |
A | ALA258 |
A | HOH708 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GOL A 610 |
Chain | Residue |
A | TRP10 |
A | PRO11 |
A | GLY219 |
A | ASN220 |
A | GLY222 |
A | LEU223 |
A | HOH728 |
A | HOH839 |
A | HOH909 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue ACT A 611 |
Chain | Residue |
A | ARG68 |
B | ACT611 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue ACT A 612 |
Chain | Residue |
A | LEU172 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue ACT A 613 |
Chain | Residue |
A | LYS330 |
A | ASP331 |
A | ARG365 |
B | LYS148 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 614 |
Chain | Residue |
A | LEU167 |
A | GLN168 |
A | HOH753 |
B | THR211 |
B | ASP213 |
site_id | AD6 |
Number of Residues | 8 |
Details | binding site for residue GOL A 615 |
Chain | Residue |
A | GLU102 |
A | ASN105 |
A | LYS123 |
A | ASP227 |
A | THR228 |
A | ARG231 |
A | ARG412 |
A | GOL608 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue ACT A 616 |
Chain | Residue |
A | LYS148 |
A | ASN149 |
A | LYS157 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue GOL A 617 |
Chain | Residue |
A | ASN235 |
A | ALA237 |
A | PHE419 |
A | GLN423 |
A | PRO429 |
A | HOH718 |
A | HOH730 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue ACT A 618 |
Chain | Residue |
A | LYS335 |
B | ARG341 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue GOL A 619 |
Chain | Residue |
A | GLN26 |
A | ACT620 |
A | HOH705 |
A | THR23 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue ACT A 620 |
Chain | Residue |
A | GLN26 |
A | GOL619 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue RU B 601 |
Chain | Residue |
B | 6RP602 |
B | CL603 |
B | CMO604 |
B | HOH703 |
site_id | AE4 |
Number of Residues | 11 |
Details | binding site for residue 6RP B 602 |
Chain | Residue |
B | TYR22 |
B | MET27 |
B | TRP100 |
B | ARG137 |
B | TRP398 |
B | TYR402 |
B | RU601 |
B | CL603 |
B | CMO604 |
B | HOH703 |
B | HOH752 |
site_id | AE5 |
Number of Residues | 3 |
Details | binding site for residue CL B 603 |
Chain | Residue |
B | RU601 |
B | 6RP602 |
B | CMO604 |
site_id | AE6 |
Number of Residues | 5 |
Details | binding site for residue CMO B 604 |
Chain | Residue |
B | ARG137 |
B | RU601 |
B | 6RP602 |
B | CL603 |
B | GOL609 |
site_id | AE7 |
Number of Residues | 7 |
Details | binding site for residue GOL B 605 |
Chain | Residue |
B | TRP10 |
B | PRO11 |
B | GLY219 |
B | ASN220 |
B | GLY222 |
B | LEU223 |
B | GOL610 |
site_id | AE8 |
Number of Residues | 7 |
Details | binding site for residue GOL B 606 |
Chain | Residue |
B | GLU221 |
B | VAL249 |
B | SER353 |
B | MET356 |
B | PHE394 |
B | ARG396 |
B | HOH716 |
site_id | AE9 |
Number of Residues | 5 |
Details | binding site for residue GOL B 607 |
Chain | Residue |
A | ARG384 |
A | ARG389 |
B | LEU430 |
B | ARG457 |
B | HOH787 |
site_id | AF1 |
Number of Residues | 7 |
Details | binding site for residue GOL B 608 |
Chain | Residue |
A | LYS314 |
A | ALA317 |
A | LEU318 |
A | LYS321 |
B | GLU376 |
B | ARG384 |
B | HOH759 |
site_id | AF2 |
Number of Residues | 7 |
Details | binding site for residue GOL B 609 |
Chain | Residue |
B | TRP10 |
B | GLN26 |
B | MET27 |
B | PHE28 |
B | THR490 |
B | CMO604 |
B | HOH739 |
site_id | AF3 |
Number of Residues | 8 |
Details | binding site for residue GOL B 610 |
Chain | Residue |
B | ASN220 |
B | GLU247 |
B | ARG396 |
B | ALA489 |
B | THR490 |
B | GOL605 |
B | HOH727 |
B | HOH947 |
site_id | AF4 |
Number of Residues | 2 |
Details | binding site for residue ACT B 611 |
Chain | Residue |
A | ACT611 |
B | ARG68 |
site_id | AF5 |
Number of Residues | 4 |
Details | binding site for residue ACT B 612 |
Chain | Residue |
A | HIS239 |
B | TYR300 |
B | GLN448 |
B | HOH707 |
site_id | AF6 |
Number of Residues | 6 |
Details | binding site for residue GOL B 613 |
Chain | Residue |
A | ASP43 |
B | GLN241 |
B | ASN482 |
B | PRO484 |
B | TYR485 |
B | HOH830 |
site_id | AF7 |
Number of Residues | 6 |
Details | binding site for residue GOL B 614 |
Chain | Residue |
B | PHE209 |
B | GLU210 |
B | GLY212 |
B | ILE214 |
B | LYS477 |
B | HOH857 |
Functional Information from PROSITE/UniProt
site_id | PS01040 |
Number of Residues | 23 |
Details | SBP_BACTERIAL_5 Bacterial extracellular solute-binding proteins, family 5 signature. AkswthseDgkTWtFtLRDDVKF |
Chain | Residue | Details |
A | ALA51-PHE73 |