Zinc in PDB 3hq2: Bsucp Crystal Structure

The structure of Bsucp Crystal Structure, PDB code: 3hq2 was solved by M.M.Lee, C.E.Isaza, J.D.White, R.P.-Y.Chen, G.F.-C.Liang, H.T.-F.He, S.I.Chan, M.K.Chan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.37 / 2.90
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	88.957, 149.002, 217.840, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 25.1

The structure of Bsucp Crystal Structure also contains other interesting chemical elements:

Fluorine	(F)	1 atom
Chlorine	(Cl)	7 atoms

The binding sites of Zinc atom in the Bsucp Crystal Structure (pdb code 3hq2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 7 binding sites of Zinc where determined in the Bsucp Crystal Structure, PDB code: 3hq2:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7;

Zinc binding site 1 out of 7 in the Bsucp Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Bsucp Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:38.4 occ:1.00 NE2 A:HIS269 2.0 25.4 1.0 OE2 A:GLU295 2.2 27.8 1.0 NE2 A:HIS265 2.2 26.0 1.0 O2 A:PO4503 2.4 43.6 1.0 O1 A:PO4503 2.4 41.6 1.0 OE1 A:GLU295 2.7 22.8 1.0 CD A:GLU295 2.8 24.2 1.0 P A:PO4503 2.9 41.4 1.0 CE1 A:HIS269 3.0 21.7 1.0 CE1 A:HIS265 3.1 26.3 1.0 CD2 A:HIS269 3.1 20.9 1.0 CD2 A:HIS265 3.3 23.1 1.0 OG A:SER298 3.8 12.2 1.0 CE2 A:TYR420 3.9 29.7 1.0 O4 A:PO4503 3.9 42.3 1.0 O3 A:PO4503 4.0 42.7 1.0 CB A:SER298 4.1 12.6 1.0 ND1 A:HIS269 4.2 19.0 1.0 CG A:HIS269 4.2 19.6 1.0 OH A:TYR420 4.2 29.4 1.0 ND1 A:HIS265 4.3 24.9 1.0 CG A:GLU295 4.3 22.6 1.0 CG A:HIS265 4.4 23.3 1.0 O A:HOH556 4.4 28.8 1.0 CZ A:TYR420 4.5 30.0 1.0 OE2 A:GLU266 4.8 21.7 1.0 OE1 A:GLU266 4.8 20.9 1.0 CD2 A:TYR420 4.8 26.8 1.0 OH A:TYR416 4.9 24.3 1.0

Zinc binding site 2 out of 7 in the Bsucp Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Bsucp Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn504 b:45.0 occ:1.00 NE2 A:HIS28 2.1 30.2 1.0 OE1 A:GLU114 2.1 34.5 1.0 CL A:CL509 2.4 40.0 1.0 CL A:CL505 2.5 39.9 1.0 CD A:GLU114 2.8 28.9 1.0 CE1 A:HIS28 2.8 23.6 1.0 OE2 A:GLU114 2.9 28.8 1.0 CD2 A:HIS28 3.3 22.2 1.0 ND1 A:HIS28 4.1 21.9 1.0 CG A:GLU114 4.3 27.8 1.0 CG A:HIS28 4.3 20.2 1.0 NE A:ARG32 4.5 27.0 1.0 CG2 A:VAL407 4.5 24.8 1.0 O A:HOH563 4.7 19.3 1.0 CD A:ARG32 4.7 23.5 1.0 CG A:ARG32 4.7 21.2 1.0

Zinc binding site 3 out of 7 in the Bsucp Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Bsucp Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn506 b:53.8 occ:0.50 CL A:CL510 2.1 53.4 0.5 CL A:CL507 2.1 54.7 0.5 ZN A:ZN508 2.1 49.8 1.0 NE2 A:HIS310 2.3 50.4 1.0 CD2 A:HIS310 3.2 45.9 1.0 CE1 A:HIS310 3.2 46.6 1.0 NZ A:LYS309 4.2 41.9 1.0 ND1 A:HIS310 4.3 45.1 1.0 CG A:HIS310 4.4 44.0 1.0 OE2 A:GLU446 4.6 47.9 1.0 OD2 A:ASP442 4.8 38.0 1.0

Zinc binding site 4 out of 7 in the Bsucp Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Bsucp Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn508 b:49.8 occ:1.00 ZN A:ZN506 2.1 53.8 0.5 CL A:CL507 3.0 54.7 0.5 CL A:CL510 3.1 53.4 0.5 NZ A:LYS309 3.1 41.9 1.0 NE2 A:HIS310 3.4 50.4 1.0 CE1 A:HIS310 3.6 46.6 1.0 CE A:LYS309 4.2 39.4 1.0 CD2 A:HIS310 4.7 45.9 1.0 ND1 A:HIS310 4.9 45.1 1.0

Zinc binding site 5 out of 7 in the Bsucp Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Bsucp Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:33.8 occ:1.00 NE2 B:HIS269 2.0 25.2 1.0 NE2 B:HIS265 2.1 22.8 1.0 OE2 B:GLU295 2.3 23.1 1.0 O2 B:PO4503 2.4 35.4 1.0 O1 B:PO4503 2.5 36.4 1.0 OE1 B:GLU295 2.6 21.4 1.0 CD B:GLU295 2.8 22.8 1.0 P B:PO4503 2.9 34.4 1.0 CE1 B:HIS269 2.9 24.6 1.0 CD2 B:HIS265 3.1 19.0 1.0 CD2 B:HIS269 3.2 22.3 1.0 CE1 B:HIS265 3.2 19.9 1.0 OG B:SER298 3.5 22.6 1.0 O4 B:PO4503 3.8 36.3 1.0 CE2 B:TYR420 3.9 17.7 1.0 CB B:SER298 4.0 19.9 1.0 ND1 B:HIS269 4.1 23.4 1.0 O3 B:PO4503 4.1 35.2 1.0 CG B:HIS269 4.2 22.1 1.0 OH B:TYR420 4.3 13.3 1.0 CG B:HIS265 4.3 18.8 1.0 CG B:GLU295 4.3 21.5 1.0 ND1 B:HIS265 4.3 18.9 1.0 CZ B:TYR420 4.5 14.9 1.0 CD2 B:TYR420 4.8 18.2 1.0 O B:HOH615 4.8 34.0 1.0 OH B:TYR416 4.8 35.6 1.0 OE1 B:GLU266 5.0 21.4 1.0 OE2 B:GLU266 5.0 23.1 1.0

Zinc binding site 6 out of 7 in the Bsucp Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Bsucp Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn504 b:42.5 occ:1.00 OE1 B:GLU114 2.1 30.4 1.0 NE2 B:HIS28 2.1 31.2 1.0 CL B:CL506 2.3 40.6 1.0 CL B:CL505 2.5 32.6 1.0 OE2 B:GLU114 2.7 26.1 1.0 CD B:GLU114 2.7 25.1 1.0 CE1 B:HIS28 3.0 24.8 1.0 CD2 B:HIS28 3.3 25.0 1.0 CG B:GLU114 4.1 22.9 1.0 ND1 B:HIS28 4.2 23.8 1.0 CG B:HIS28 4.3 23.2 1.0 CG2 B:VAL407 4.5 23.8 1.0 NE B:ARG32 4.6 27.5 1.0 O B:HOH519 4.6 26.3 1.0 CG B:ARG32 4.8 22.3 1.0 CD B:ARG32 4.9 24.6 1.0

Zinc binding site 7 out of 7 in the Bsucp Crystal Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Bsucp Crystal Structure within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn507 b:46.0 occ:1.00 OE1 B:GLU449 2.3 32.1 1.0 ND1 B:HIS451 2.3 17.1 1.0 CL B:CL508 2.4 33.0 1.0 CE1 B:HIS451 2.7 17.0 1.0 OE2 B:GLU449 2.7 30.8 1.0 CD B:GLU449 2.8 31.3 1.0 CG B:HIS451 3.5 16.9 1.0 NE2 B:HIS451 3.9 16.8 1.0 CB B:HIS451 4.3 19.3 1.0 CG B:GLU449 4.3 28.3 1.0 CD2 B:HIS451 4.3 15.6 1.0 N B:HIS451 4.8 22.3 1.0 CA B:GLU449 4.9 25.7 1.0 CB B:GLU449 5.0 25.3 1.0

M.M.Lee, C.E.Isaza, J.D.White, R.P.Chen, G.F.Liang, H.T.He, S.I.Chan, M.K.Chan. Insight Into the Substrate Length Restriction of M32 Carboxypeptidases: Characterization of Two Distinct Subfamilies. Proteins V. 77 647 2009.
ISSN: ISSN 0887-3585
PubMed: 19544567
DOI: 10.1002/PROT.22478