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 | 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 | 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 |