Zinc in PDB 6l7g: Metallo Beta-Lactamase Fold Protein (Camp Bound)

The structure of Metallo Beta-Lactamase Fold Protein (Camp Bound), PDB code: 6l7g was solved by K.-Y.Lee, D.-G.Kim, B.-J.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.85 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.734, 121.521, 187.256, 90, 90, 90
R / Rfree (%)	17.7 / 20.8

The structure of Metallo Beta-Lactamase Fold Protein (Camp Bound) also contains other interesting chemical elements:

Nickel	(Ni)	12 atoms
Caesium	(Cs)	6 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Zinc atom in the Metallo Beta-Lactamase Fold Protein (Camp Bound) (pdb code 6l7g). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 12 binding sites of Zinc where determined in the Metallo Beta-Lactamase Fold Protein (Camp Bound), PDB code: 6l7g:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn305 b:25.7 occ:0.50 NI A:NI303 0.0 25.1 0.5 O A:HOH409 2.1 25.2 1.0 NE2 A:HIS110 2.1 18.3 1.0 ND1 A:HIS50 2.1 22.2 1.0 NE2 A:HIS48 2.2 19.1 1.0 OD2 A:ASP144 2.5 22.2 1.0 O A:HOH534 2.6 37.5 1.0 CD2 A:HIS110 3.0 19.6 1.0 CE1 A:HIS50 3.0 22.7 1.0 CD2 A:HIS48 3.1 18.1 1.0 CE1 A:HIS110 3.1 18.4 1.0 CG A:HIS50 3.2 23.1 1.0 NI A:NI304 3.2 25.3 0.5 ZN A:ZN306 3.3 25.9 0.5 CE1 A:HIS48 3.3 18.9 1.0 CG A:ASP144 3.4 22.4 1.0 CB A:HIS50 3.6 22.0 1.0 O A:HOH516 3.8 28.9 1.0 CB A:ASP144 3.8 18.7 1.0 NE2 A:HIS53 4.0 21.0 1.0 CD2 A:HIS53 4.1 24.1 1.0 O C:HOH510 4.1 25.2 1.0 CG A:HIS110 4.2 18.2 1.0 ND1 A:HIS110 4.2 19.1 1.0 NE2 A:HIS50 4.2 21.4 1.0 CD2 A:HIS50 4.3 22.1 1.0 CG A:HIS48 4.3 17.4 1.0 ND1 A:HIS48 4.3 17.9 1.0 OD1 A:ASP52 4.4 24.8 1.0 OD1 A:ASP144 4.5 18.7 1.0 OD2 A:ASP52 4.8 23.9 1.0 O A:SER111 4.8 19.7 1.0 CE1 A:HIS53 5.0 23.6 1.0 CA A:HIS50 5.0 21.0 1.0 CG A:ASP52 5.0 25.3 1.0

Zinc binding site 2 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn306 b:25.9 occ:0.50 NI A:NI304 0.0 25.3 0.5 O A:HOH409 2.0 25.2 1.0 NE2 A:HIS53 2.2 21.0 1.0 NE2 A:HIS195 2.2 21.9 1.0 OD2 A:ASP144 2.2 22.2 1.0 OD2 A:ASP52 2.2 23.9 1.0 O A:HOH516 2.4 28.9 1.0 CG A:ASP144 3.0 22.4 1.0 CD2 A:HIS195 3.1 21.4 1.0 CD2 A:HIS53 3.1 24.1 1.0 CG A:ASP52 3.2 25.3 1.0 CE1 A:HIS195 3.2 23.3 1.0 CE1 A:HIS53 3.2 23.6 1.0 NI A:NI303 3.2 25.1 0.5 OD1 A:ASP144 3.2 18.7 1.0 ZN A:ZN305 3.3 25.7 0.5 OD1 A:ASP52 3.5 24.8 1.0 O A:HOH534 3.6 37.5 1.0 O A:HOH535 4.0 37.8 1.0 OE1 A:GLN8 4.1 26.8 1.0 NE2 A:HIS48 4.2 19.1 1.0 CG A:HIS195 4.2 19.8 1.0 CG A:HIS53 4.3 22.2 1.0 ND1 A:HIS195 4.3 22.2 1.0 CE1 A:HIS48 4.3 18.9 1.0 ND1 A:HIS53 4.3 24.6 1.0 CB A:ASP144 4.4 18.7 1.0 CB A:ASP52 4.5 25.8 1.0 NE2 A:HIS110 4.7 18.3 1.0 CD A:GLN8 4.8 23.6 1.0

Zinc binding site 3 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn306 b:23.7 occ:0.50 NI B:NI304 0.0 22.7 0.5 O B:HOH459 1.8 23.1 1.0 NE2 B:HIS48 2.1 16.7 1.0 NE2 B:HIS110 2.1 17.5 1.0 ND1 B:HIS50 2.1 19.2 1.0 OD2 B:ASP144 2.5 18.6 1.0 O B:HOH556 2.8 38.0 1.0 CD2 B:HIS110 3.0 16.6 1.0 CE1 B:HIS50 3.0 19.6 1.0 CD2 B:HIS48 3.0 17.8 1.0 CE1 B:HIS48 3.1 19.0 1.0 CE1 B:HIS110 3.1 17.7 1.0 CG B:HIS50 3.2 19.9 1.0 NI B:NI305 3.3 22.9 0.5 ZN B:ZN307 3.3 23.9 0.5 CB B:HIS50 3.5 21.5 1.0 CG B:ASP144 3.5 21.0 1.0 O B:HOH525 3.8 32.7 1.0 CB B:ASP144 3.9 16.8 1.0 O A:HOH523 4.0 21.8 1.0 NE2 B:HIS53 4.0 17.9 1.0 CG B:HIS110 4.2 16.9 1.0 CD2 B:HIS53 4.2 20.4 1.0 NE2 B:HIS50 4.2 19.5 1.0 CG B:HIS48 4.2 16.5 1.0 ND1 B:HIS110 4.2 16.8 1.0 ND1 B:HIS48 4.2 18.3 1.0 CD2 B:HIS50 4.3 19.9 1.0 OD1 B:ASP52 4.4 21.7 1.0 OD1 B:ASP144 4.6 21.4 1.0 O B:SER111 4.7 17.6 1.0 OD2 B:ASP52 4.8 21.8 1.0 CE1 B:HIS53 4.9 19.8 1.0 CA B:HIS50 4.9 21.1 1.0

Zinc binding site 4 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn307 b:23.9 occ:0.50 NI B:NI305 0.0 22.9 0.5 O B:HOH459 2.1 23.1 1.0 NE2 B:HIS53 2.1 17.9 1.0 OD2 B:ASP144 2.1 18.6 1.0 NE2 B:HIS195 2.2 18.5 1.0 OD2 B:ASP52 2.2 21.8 1.0 O B:HOH525 2.4 32.7 1.0 CG B:ASP144 3.0 21.0 1.0 CD2 B:HIS53 3.1 20.4 1.0 CD2 B:HIS195 3.1 20.1 1.0 CE1 B:HIS53 3.1 19.8 1.0 CE1 B:HIS195 3.2 17.5 1.0 CG B:ASP52 3.2 23.5 1.0 NI B:NI304 3.3 22.7 0.5 OD1 B:ASP144 3.3 21.4 1.0 ZN B:ZN306 3.3 23.7 0.5 OD1 B:ASP52 3.5 21.7 1.0 O B:HOH556 3.7 38.0 1.0 OE1 B:GLN8 4.1 26.2 1.0 NE2 B:HIS48 4.2 16.7 1.0 CE1 B:HIS48 4.2 19.0 1.0 CG B:HIS53 4.2 20.2 1.0 ND1 B:HIS53 4.2 20.3 1.0 ND1 B:HIS195 4.2 19.7 1.0 CG B:HIS195 4.2 18.9 1.0 CB B:ASP144 4.4 16.8 1.0 CB B:ASP52 4.5 22.2 1.0 NE2 B:HIS110 4.7 17.5 1.0 CD B:GLN8 4.8 20.7 1.0

Zinc binding site 5 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn305 b:26.8 occ:0.50 NI C:NI303 0.0 26.5 0.5 O C:HOH406 2.1 22.2 1.0 NE2 C:HIS110 2.1 18.1 1.0 ND1 C:HIS50 2.1 22.9 1.0 NE2 C:HIS48 2.2 19.5 1.0 OD2 C:ASP144 2.5 22.0 1.0 O C:HOH515 2.8 35.1 1.0 CD2 C:HIS110 3.0 20.0 1.0 CD2 C:HIS48 3.0 18.9 1.0 CE1 C:HIS50 3.1 25.0 1.0 CE1 C:HIS110 3.1 19.0 1.0 CG C:HIS50 3.2 25.6 1.0 NI C:NI304 3.2 27.4 0.5 ZN C:ZN306 3.3 27.4 0.5 CE1 C:HIS48 3.3 19.2 1.0 CB C:HIS50 3.5 25.6 1.0 CG C:ASP144 3.5 23.7 1.0 O C:HOH513 3.8 38.0 1.0 CB C:ASP144 3.9 18.8 1.0 CG C:HIS110 4.1 17.7 1.0 NE2 C:HIS53 4.1 23.7 1.0 O B:HOH493 4.1 22.3 1.0 ND1 C:HIS110 4.2 16.3 1.0 CD2 C:HIS53 4.2 25.7 1.0 NE2 C:HIS50 4.2 24.2 1.0 CG C:HIS48 4.2 17.2 1.0 CD2 C:HIS50 4.3 26.6 1.0 OD1 C:ASP52 4.3 26.7 1.0 ND1 C:HIS48 4.4 19.2 1.0 OD1 C:ASP144 4.6 24.0 1.0 OD2 C:ASP52 4.7 28.3 1.0 O C:SER111 4.7 21.8 1.0 CA C:HIS50 4.9 24.6 1.0 CG C:ASP52 5.0 30.6 1.0

Zinc binding site 6 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn306 b:27.4 occ:0.50 NI C:NI304 0.0 27.4 0.5 O C:HOH406 1.9 22.2 1.0 OD2 C:ASP144 2.1 22.0 1.0 NE2 C:HIS195 2.2 22.2 1.0 NE2 C:HIS53 2.2 23.7 1.0 OD2 C:ASP52 2.3 28.3 1.0 O C:HOH513 2.6 38.0 1.0 CG C:ASP144 3.0 23.7 1.0 CD2 C:HIS195 3.1 22.9 1.0 CD2 C:HIS53 3.1 25.7 1.0 CE1 C:HIS195 3.2 22.1 1.0 CG C:ASP52 3.2 30.6 1.0 NI C:NI303 3.2 26.5 0.5 OD1 C:ASP144 3.3 24.0 1.0 ZN C:ZN305 3.3 26.8 0.5 CE1 C:HIS53 3.3 25.1 1.0 OD1 C:ASP52 3.5 26.7 1.0 O C:HOH515 3.9 35.1 1.0 OE1 C:GLN8 4.0 29.1 1.0 NE2 C:HIS48 4.1 19.5 1.0 CG C:HIS195 4.2 19.9 1.0 ND1 C:HIS195 4.3 21.9 1.0 CE1 C:HIS48 4.3 19.2 1.0 CG C:HIS53 4.3 22.9 1.0 ND1 C:HIS53 4.4 24.1 1.0 CB C:ASP144 4.4 18.8 1.0 CB C:ASP52 4.5 26.7 1.0 NE2 C:HIS110 4.6 18.1 1.0 CD C:GLN8 4.7 24.7 1.0 CG C:GLN8 5.0 22.8 1.0

Zinc binding site 7 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn306 b:23.2 occ:0.50 NI D:NI304 0.0 22.2 0.5 O D:HOH416 2.0 24.8 1.0 NE2 D:HIS110 2.1 17.2 1.0 ND1 D:HIS50 2.1 19.6 1.0 NE2 D:HIS48 2.1 16.3 1.0 OD2 D:ASP144 2.5 19.2 1.0 O D:HOH536 2.6 35.4 1.0 CD2 D:HIS110 3.0 15.7 1.0 CD2 D:HIS48 3.0 17.1 1.0 CE1 D:HIS50 3.1 18.5 1.0 CG D:HIS50 3.2 18.2 1.0 CE1 D:HIS110 3.2 17.1 1.0 CE1 D:HIS48 3.2 17.6 1.0 NI D:NI305 3.3 23.3 0.5 ZN D:ZN307 3.3 24.2 0.5 CB D:HIS50 3.5 19.4 1.0 CG D:ASP144 3.5 19.1 1.0 CB D:ASP144 3.9 17.3 1.0 O F:HOH510 3.9 24.2 1.0 O D:HOH520 4.0 29.5 1.0 NE2 D:HIS53 4.0 19.9 1.0 CD2 D:HIS53 4.1 20.3 1.0 CG D:HIS110 4.2 16.1 1.0 CG D:HIS48 4.2 17.0 1.0 ND1 D:HIS110 4.2 17.0 1.0 NE2 D:HIS50 4.2 19.0 1.0 ND1 D:HIS48 4.3 17.1 1.0 CD2 D:HIS50 4.3 20.3 1.0 OD1 D:ASP52 4.4 21.2 1.0 OD1 D:ASP144 4.5 22.2 1.0 OD2 D:ASP52 4.7 21.4 1.0 O D:SER111 4.7 17.1 1.0 CA D:HIS50 4.9 20.1 1.0 CG D:ASP52 5.0 21.8 1.0 CE1 D:HIS53 5.0 22.1 1.0

Zinc binding site 8 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn307 b:24.2 occ:0.50 NI D:NI305 0.0 23.3 0.5 O D:HOH416 2.0 24.8 1.0 NE2 D:HIS53 2.1 19.9 1.0 NE2 D:HIS195 2.1 19.5 1.0 OD2 D:ASP144 2.2 19.2 1.0 OD2 D:ASP52 2.2 21.4 1.0 O D:HOH520 2.5 29.5 1.0 CD2 D:HIS53 3.0 20.3 1.0 CG D:ASP144 3.0 19.1 1.0 CD2 D:HIS195 3.0 18.4 1.0 CE1 D:HIS195 3.1 19.3 1.0 CG D:ASP52 3.1 21.8 1.0 CE1 D:HIS53 3.2 22.1 1.0 OD1 D:ASP144 3.3 22.2 1.0 NI D:NI304 3.3 22.2 0.5 ZN D:ZN306 3.3 23.2 0.5 OD1 D:ASP52 3.5 21.2 1.0 O D:HOH536 3.6 35.4 1.0 OE1 D:GLN8 4.0 25.9 1.0 O D:HOH544 4.1 35.7 1.0 NE2 D:HIS48 4.2 16.3 1.0 CG D:HIS53 4.2 22.1 1.0 CG D:HIS195 4.2 18.0 1.0 ND1 D:HIS195 4.2 19.9 1.0 ND1 D:HIS53 4.3 19.4 1.0 CE1 D:HIS48 4.3 17.6 1.0 CB D:ASP144 4.4 17.3 1.0 CB D:ASP52 4.5 21.5 1.0 NE2 D:HIS110 4.7 17.2 1.0 CD D:GLN8 4.8 21.2 1.0

Zinc binding site 9 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn305 b:24.1 occ:0.50 NI E:NI303 0.0 23.3 0.5 O E:HOH411 2.0 24.4 1.0 NE2 E:HIS110 2.0 17.7 1.0 ND1 E:HIS50 2.2 19.8 1.0 NE2 E:HIS48 2.2 18.1 1.0 OD2 E:ASP144 2.5 19.5 1.0 O E:HOH517 2.6 36.9 1.0 CD2 E:HIS110 2.9 16.4 1.0 CD2 E:HIS48 3.1 17.6 1.0 CE1 E:HIS110 3.1 17.3 1.0 CE1 E:HIS50 3.1 17.5 1.0 CG E:HIS50 3.2 20.6 1.0 NI E:NI304 3.2 23.1 0.5 ZN E:ZN306 3.3 24.3 0.5 CE1 E:HIS48 3.3 18.8 1.0 CG E:ASP144 3.5 18.0 1.0 CB E:HIS50 3.6 23.2 1.0 CB E:ASP144 3.9 15.3 1.0 O E:HOH514 3.9 37.1 1.0 NE2 E:HIS53 4.0 20.3 1.0 CG E:HIS110 4.1 16.4 1.0 CD2 E:HIS53 4.1 23.3 1.0 ND1 E:HIS110 4.1 15.6 1.0 NE2 E:HIS50 4.3 18.0 1.0 O D:HOH488 4.3 19.3 1.0 CG E:HIS48 4.3 16.0 1.0 CD2 E:HIS50 4.3 18.2 1.0 ND1 E:HIS48 4.4 18.0 1.0 OD1 E:ASP52 4.4 22.6 1.0 OD1 E:ASP144 4.6 20.4 1.0 OD2 E:ASP52 4.6 22.1 1.0 O E:SER111 4.8 18.4 1.0 CG E:ASP52 4.9 23.9 1.0 CE1 E:HIS53 5.0 20.9 1.0 CA E:HIS50 5.0 21.4 1.0

Zinc binding site 10 out of 12 in the Metallo Beta-Lactamase Fold Protein (Camp Bound)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Metallo Beta-Lactamase Fold Protein (Camp Bound) within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn306 b:24.3 occ:0.50 NI E:NI304 0.0 23.1 0.5 O E:HOH411 2.0 24.4 1.0 NE2 E:HIS53 2.1 20.3 1.0 OD2 E:ASP52 2.2 22.1 1.0 CE1 E:HIS195 2.2 17.7 1.0 OD2 E:ASP144 2.2 19.5 1.0 O E:HOH514 2.6 37.1 1.0 CD2 E:HIS53 3.0 23.3 1.0 CG E:ASP144 3.1 18.0 1.0 ND1 E:HIS195 3.1 22.5 1.0 NE2 E:HIS195 3.1 21.7 1.0 CG E:ASP52 3.1 23.9 1.0 CE1 E:HIS53 3.2 20.9 1.0 NI E:NI303 3.2 23.3 0.5 ZN E:ZN305 3.3 24.1 0.5 OD1 E:ASP144 3.3 20.4 1.0 OD1 E:ASP52 3.5 22.6 1.0 O E:HOH517 3.8 36.9 1.0 OE1 E:GLN8 4.1 23.9 1.0 NE2 E:HIS48 4.1 18.1 1.0 CG E:HIS53 4.2 22.0 1.0 CD2 E:HIS195 4.3 17.5 1.0 CE1 E:HIS48 4.3 18.8 1.0 CG E:HIS195 4.3 17.9 1.0 ND1 E:HIS53 4.3 22.9 1.0 CB E:ASP144 4.4 15.3 1.0 CB E:ASP52 4.4 23.6 1.0 NE2 E:HIS110 4.6 17.7 1.0 CD E:GLN8 4.8 22.6 1.0 CG E:GLN8 5.0 21.8 1.0 CE1 E:HIS110 5.0 17.3 1.0

K.-Y.Lee, D.-G.Kim, B.-J.Lee. Metallo Beta-Lactamase Fold Protein To Be Published.