6GT2
Reduced copper nitrite reductase from Achromobacter cycloclastes determined by serial femtosecond rotation crystallography
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 501 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 502 |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| A | ILE257 |
| A | HIS306 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue MLI A 503 |
| Chain | Residue |
| A | ARG250 |
| A | ASP251 |
| A | ARG253 |
| A | ASN307 |
| A | GLU310 |
| A | MLI504 |
| A | MLI504 |
| A | HOH660 |
| A | HOH660 |
| A | HOH726 |
| A | HOH726 |
| A | HOH726 |
| A | ARG250 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MLI A 504 |
| Chain | Residue |
| A | LEU213 |
| A | ARG250 |
| A | ARG250 |
| A | MLI503 |
| A | MLI503 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue MLI A 505 |
| Chain | Residue |
| A | GLU77 |
| A | THR127 |
| A | LYS128 |
| A | ARG271 |
| A | ASP277 |
| A | HOH601 |
| A | HOH603 |
| A | HOH674 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MLI A 506 |
| Chain | Residue |
| A | VAL142 |
| A | ILE257 |
| A | ALA302 |
| A | PHE312 |
| A | HOH619 |
| A | HOH658 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue MLI A 507 |
| Chain | Residue |
| A | LEU93 |
| A | LEU94 |
| A | GLY200 |
| A | VAL237 |
| A | GLY324 |
| A | GLU325 |
| A | HOH679 |
| A | HOH815 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue MLI A 508 |
| Chain | Residue |
| A | THR228 |
| A | GLY229 |
| A | HIS319 |
| A | LYS321 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MLI A 509 |
| Chain | Residue |
| A | GLY225 |
| A | PHE312 |
| A | HIS319 |
| A | HOH605 |
| A | HOH698 |
| A | HOH732 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue MLI A 510 |
| Chain | Residue |
| A | LYS174 |
| A | TYR203 |
| A | GLU204 |
| A | THR234 |
| A | ALA235 |
| A | ALA236 |
| A | GLU239 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 164 |
| Details | Domain: {"description":"Plastocyanin-like 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"type 1 copper site"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"description":"type 2 copper site"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| 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 |
