2BW4
Atomic Resolution Structure of Resting State of the Achromobacter cycloclastes Cu Nitrite Reductase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005507 | molecular_function | copper ion binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019333 | biological_process | denitrification pathway |
A | 0042128 | biological_process | nitrate assimilation |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
A | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU A 501 |
Chain | Residue |
A | HIS100 |
A | HIS135 |
A | HIS306 |
A | HOH2276 |
A | HOH2552 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CU A 500 |
Chain | Residue |
A | HIS95 |
A | CYS136 |
A | HIS145 |
A | MET150 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 503 |
Chain | Residue |
A | THR228 |
A | GLY229 |
A | HIS319 |
A | LYS321 |
A | HOH2616 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ACT A 504 |
Chain | Residue |
A | GLY225 |
A | PHE312 |
A | ALA317 |
A | HIS319 |
A | HOH2617 |
A | HOH2618 |
A | HOH2619 |
A | HOH2620 |
A | HOH2622 |
A | HOH2623 |
A | HOH2624 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 A 505 |
Chain | Residue |
A | PRO158 |
A | ARG159 |
A | ASP160 |
A | HOH2356 |
A | HOH2625 |
A | HOH2626 |
A | HOH2627 |
A | HOH2628 |
A | HOH2629 |
A | HOH2630 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 506 |
Chain | Residue |
A | LYS33 |
A | ASP188 |
A | GLU189 |
A | LYS194 |
A | HOH2043 |
A | HOH2414 |
A | HOH2631 |
A | HOH2632 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACT A 507 |
Chain | Residue |
A | VAL243 |
A | LEU256 |
A | HIS260 |
A | GLY261 |
A | ALA291 |
A | PHE292 |
A | TYR293 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACT A 508 |
Chain | Residue |
A | TRP265 |
A | THR267 |
A | GLY268 |
A | LYS269 |
A | ASN272 |
A | GLN278 |
A | HOH2512 |
A | HOH2633 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE MLI A 502 |
Chain | Residue |
A | ARG250 |
A | ARG250 |
A | ASP251 |
A | ARG253 |
A | ASN307 |
A | GLU310 |
A | HOH2612 |
A | HOH2612 |
A | HOH2612 |
A | HOH2613 |
A | HOH2613 |
A | HOH2614 |
A | HOH2615 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: type 1 copper site |
Chain | Residue | Details |
A | HIS95 | |
A | CYS136 | |
A | HIS145 | |
A | MET150 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: type 2 copper site |
Chain | Residue | Details |
A | HIS100 | |
A | HIS135 | |
A | HIS306 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nid |
Chain | Residue | Details |
A | PHE64 | |
A | GLY66 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1nid |
Chain | Residue | Details |
A | ASP98 | |
A | HIS255 |
site_id | MCSA1 |
Number of Residues | 11 |
Details | M-CSA 4 |
Chain | Residue | Details |
A | HIS95 | metal ligand |
A | THR280 | electrostatic stabiliser, modifies pKa |
A | HIS306 | metal ligand |
A | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
A | HIS100 | metal ligand |
A | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
A | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
A | HIS145 | metal ligand |
A | MET150 | metal ligand |
A | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU279 | electrostatic stabiliser, modifies pKa |