5ON0
Crystal structure of NikA in complex with Fe-L2 (N-(2-hydroxy-3methoxybenzyl)-N-N'-ethylenediaminediacetic acid)
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 | 9YH602 |
A | HOH1060 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue 9YH A 602 |
Chain | Residue |
A | FE601 |
A | GOL608 |
A | HOH702 |
A | HOH803 |
A | HOH832 |
A | TYR22 |
A | MET27 |
A | ARG97 |
A | TRP100 |
A | ARG137 |
A | TRP398 |
A | HIS416 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ACT A 603 |
Chain | Residue |
A | ARG68 |
A | ASP69 |
A | ASP70 |
A | HOH704 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ACT A 604 |
Chain | Residue |
A | ASN261 |
A | GLU262 |
A | LEU263 |
A | HOH1033 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ACT A 605 |
Chain | Residue |
A | ASN235 |
A | ALA237 |
A | GLN423 |
A | HOH715 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 606 |
Chain | Residue |
A | GLU343 |
A | ARG384 |
A | ARG389 |
A | HOH816 |
B | ARG457 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue GOL A 607 |
Chain | Residue |
A | TYR485 |
A | ALA486 |
A | HOH778 |
A | HOH979 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue GOL A 608 |
Chain | Residue |
A | ASN220 |
A | GLU247 |
A | 9YH602 |
A | GOL609 |
A | HOH722 |
A | HOH766 |
A | HOH926 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue GOL A 609 |
Chain | Residue |
A | TRP10 |
A | GLY219 |
A | ASN220 |
A | GLY222 |
A | LEU223 |
A | GOL608 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GOL A 610 |
Chain | Residue |
A | GLU102 |
A | ASN105 |
A | LYS123 |
A | ASP227 |
A | THR228 |
A | HOH932 |
A | HOH964 |
A | HOH996 |
A | HOH1040 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue CL A 611 |
Chain | Residue |
A | THR23 |
A | GLN26 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue GOL A 612 |
Chain | Residue |
A | PHE209 |
A | GLY212 |
A | ILE214 |
A | TYR238 |
A | LYS477 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue GOL A 613 |
Chain | Residue |
A | GLU82 |
A | ALA85 |
A | GLU86 |
A | LYS111 |
A | ALA112 |
A | GLN366 |
A | HOH752 |
A | HOH855 |
A | HOH870 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue GOL A 614 |
Chain | Residue |
A | ASN270 |
A | LYS306 |
A | SER308 |
A | HIS459 |
A | ALA462 |
A | TYR464 |
A | HOH782 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue GOL A 615 |
Chain | Residue |
A | HIS56 |
A | HOH726 |
A | HOH956 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue CL A 616 |
Chain | Residue |
A | TYR22 |
A | ARG97 |
A | HOH751 |
site_id | AD8 |
Number of Residues | 10 |
Details | binding site for residue GOL A 617 |
Chain | Residue |
A | LEU92 |
A | ARG95 |
A | ILE107 |
A | VAL108 |
A | ASP109 |
A | VAL110 |
A | ASN281 |
A | HOH839 |
A | HOH1015 |
A | HOH1071 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue CL A 618 |
Chain | Residue |
A | ASN149 |
A | LYS157 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue ACT A 619 |
Chain | Residue |
A | ARG365 |
B | LYS148 |
B | HOH805 |
A | ASP331 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue ACT A 620 |
Chain | Residue |
A | GLN361 |
A | SER372 |
A | LEU373 |
A | HOH740 |
A | HOH912 |
site_id | AE3 |
Number of Residues | 2 |
Details | binding site for residue FE B 601 |
Chain | Residue |
B | 9YH602 |
B | HOH989 |
site_id | AE4 |
Number of Residues | 13 |
Details | binding site for residue 9YH B 602 |
Chain | Residue |
B | TYR22 |
B | MET27 |
B | ARG97 |
B | TRP100 |
B | ARG137 |
B | TYR382 |
B | TRP398 |
B | THR490 |
B | FE601 |
B | HOH732 |
B | HOH867 |
B | HOH988 |
B | HOH989 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue ACT B 603 |
Chain | Residue |
A | ASN75 |
B | THR203 |
B | PRO225 |
B | ASP227 |
site_id | AE6 |
Number of Residues | 5 |
Details | binding site for residue GOL B 604 |
Chain | Residue |
B | ALA486 |
B | ALA489 |
B | HOH705 |
B | HOH876 |
B | HOH882 |
site_id | AE7 |
Number of Residues | 8 |
Details | binding site for residue GOL B 605 |
Chain | Residue |
B | TRP10 |
B | PRO11 |
B | GLY219 |
B | ASN220 |
B | GLY222 |
B | LEU223 |
B | GOL606 |
B | HOH859 |
site_id | AE8 |
Number of Residues | 9 |
Details | binding site for residue GOL B 606 |
Chain | Residue |
B | ASN220 |
B | GLU247 |
B | ARG396 |
B | ALA489 |
B | THR490 |
B | GOL605 |
B | HOH734 |
B | HOH901 |
B | HOH993 |
site_id | AE9 |
Number of Residues | 5 |
Details | binding site for residue CL B 607 |
Chain | Residue |
B | MET27 |
B | PHE28 |
B | THR490 |
B | HOH922 |
B | HOH964 |
site_id | AF1 |
Number of Residues | 3 |
Details | binding site for residue ACT B 608 |
Chain | Residue |
B | ASN183 |
B | HOH752 |
B | HOH1007 |
site_id | AF2 |
Number of Residues | 8 |
Details | binding site for residue GOL B 609 |
Chain | Residue |
B | ASN261 |
B | LEU263 |
B | ARG266 |
B | LEU425 |
B | ALA426 |
B | GLU461 |
B | HOH711 |
B | HOH811 |
site_id | AF3 |
Number of Residues | 4 |
Details | binding site for residue ACT B 610 |
Chain | Residue |
B | HIS56 |
B | TRP63 |
B | HOH707 |
B | HOH896 |
site_id | AF4 |
Number of Residues | 2 |
Details | binding site for residue ACT B 611 |
Chain | Residue |
A | LYS335 |
B | ARG341 |
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 |