Copper in PDB 6zav: No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx)

Enzymatic activity of No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx)

Protein crystallography data

Copper Binding Sites:

Copper binding site 1 out of 2 in 6zav

Copper Binding Sites List in 6zav

Copper binding site 1 out of 2 in the No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu501 b:14.0 occ:1.00 ND1 A:HIS89 2.1 11.9 1.0 ND1 A:HIS140 2.1 12.5 1.0 SG A:CYS130 2.2 12.6 1.0 SD A:MET145 2.5 13.1 1.0 CE1 A:HIS140 3.0 12.6 1.0 CE1 A:HIS89 3.0 12.2 1.0 CG A:HIS89 3.1 11.9 1.0 CG A:HIS140 3.2 12.5 1.0 CB A:CYS130 3.2 12.7 1.0 CE A:MET145 3.3 14.2 1.0 CB A:HIS89 3.5 11.6 1.0 CB A:HIS140 3.5 11.8 1.0 CA A:HIS89 3.8 12.0 1.0 CG A:MET145 3.9 13.7 1.0 NE2 A:HIS140 4.2 13.4 1.0 NE2 A:HIS89 4.2 11.6 1.0 O A:PRO88 4.2 13.6 1.0 CD2 A:HIS140 4.2 13.7 1.0 CG A:PRO132 4.2 14.2 0.6 CD2 A:HIS89 4.2 12.2 1.0 CG A:PRO132 4.3 15.8 0.4 CB A:MET145 4.5 11.9 1.0 SD A:MET56 4.6 14.2 0.3 CD A:PRO132 4.6 11.9 0.6 CA A:CYS130 4.7 11.2 1.0 N A:ASN90 4.7 12.0 1.0 CA A:HIS140 4.7 11.3 1.0 C A:HIS89 4.8 12.2 1.0 N A:HIS89 4.9 12.5 1.0 CD A:PRO132 4.9 13.5 0.4 C A:PRO88 4.9 12.6 1.0 CE A:MET56 5.0 13.4 0.7

Copper binding site 2 out of 2 in 6zav

Copper Binding Sites List in 6zav

Copper binding site 2 out of 2 in the No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of No-Bound Copper Nitrite Reductase From Bradyrhizobium Sp. Ors 375 (Two-Domain) at 1.19 A Resolution (Unrestrained, Full Matrix Refinement By Shelx) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu502 b:13.9 occ:1.00 NE2 A:HIS129 2.0 12.0 1.0 NE2 A:HIS94 2.0 10.7 1.0 O A:NO503 2.1 23.8 0.7 N A:NO503 2.2 29.0 0.7 CD2 A:HIS129 2.9 12.1 1.0 CE1 A:HIS94 2.9 10.6 1.0 CE1 A:HIS129 3.0 12.3 1.0 CD2 A:HIS94 3.1 10.7 1.0 OD2 A:ASP92 3.7 20.6 0.8 ND1 A:HIS94 4.1 10.2 1.0 CG A:HIS129 4.1 10.7 1.0 ND1 A:HIS129 4.1 11.6 1.0 CG A:HIS94 4.2 9.7 1.0 O A:HOH629 4.2 32.6 0.5 CG A:ASP92 4.4 15.2 0.8 OD1 A:ASP92 4.6 15.6 0.8

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