3MVY
X-ray structure of the diatomic oxo-intermediate NikA/1-Int', prior hydroxylation
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 ACT A 503 |
Chain | Residue |
A | LYS52 |
A | ASP69 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 504 |
Chain | Residue |
A | ASN261 |
A | GLU262 |
A | LEU263 |
A | HOH689 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 505 |
Chain | Residue |
A | HOH680 |
A | ASN235 |
A | ALA237 |
A | GLN423 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 506 |
Chain | Residue |
A | ARG384 |
A | ARG389 |
B | LEU430 |
B | ARG457 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 507 |
Chain | Residue |
A | PRO159 |
A | LEU167 |
A | GLN168 |
A | HOH721 |
B | ALA208 |
B | THR211 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 508 |
Chain | Residue |
A | ASN149 |
A | LYS157 |
A | HOH640 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 509 |
Chain | Residue |
A | GLU358 |
A | GLN361 |
A | LEU373 |
B | HOH606 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FE A 510 |
Chain | Residue |
A | BHZ511 |
A | PER512 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE BHZ A 511 |
Chain | Residue |
A | TYR22 |
A | MET27 |
A | ARG97 |
A | TRP100 |
A | ARG137 |
A | TRP398 |
A | HIS416 |
A | THR490 |
A | FE510 |
A | PER512 |
A | HOH544 |
A | HOH612 |
A | HOH620 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PER A 512 |
Chain | Residue |
A | ARG137 |
A | FE510 |
A | BHZ511 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 513 |
Chain | Residue |
A | HIS442 |
A | ASP443 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 515 |
Chain | Residue |
A | ASN220 |
A | ILE246 |
A | GLU247 |
A | ARG396 |
A | ALA489 |
A | THR490 |
A | GOL516 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 516 |
Chain | Residue |
A | PRO11 |
A | GLY219 |
A | ASN220 |
A | GLY222 |
A | LEU223 |
A | GOL515 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 517 |
Chain | Residue |
A | ARG89 |
A | ASP109 |
A | VAL110 |
A | ASN281 |
A | HOH723 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 518 |
Chain | Residue |
A | PHE28 |
A | SER31 |
A | ARG140 |
A | GLU491 |
A | ILE492 |
A | GLU495 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT B 503 |
Chain | Residue |
B | THR23 |
B | GLN26 |
B | GLU378 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT B 504 |
Chain | Residue |
B | ASN274 |
B | LYS275 |
B | LYS276 |
B | TYR310 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 505 |
Chain | Residue |
B | PRO11 |
B | GLY219 |
B | ASN220 |
B | GLY222 |
site_id | CC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE FE B 506 |
Chain | Residue |
B | BHZ507 |
B | PER508 |
site_id | CC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE BHZ B 507 |
Chain | Residue |
B | TYR22 |
B | MET27 |
B | ARG97 |
B | TRP100 |
B | ARG137 |
B | TRP398 |
B | THR490 |
B | FE506 |
B | PER508 |
B | HOH547 |
B | HOH609 |
B | HOH669 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PER B 508 |
Chain | Residue |
B | ARG137 |
B | FE506 |
B | BHZ507 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT B 509 |
Chain | Residue |
A | ARG97 |
A | HOH596 |
B | LYS314 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 510 |
Chain | Residue |
B | GLU221 |
B | VAL249 |
B | SER353 |
B | MET356 |
B | PHE394 |
B | HIS395 |
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 |