Zinc in PDB 6btn: BMP1 Complexed with A Reverse Hydroxymate - Compound 1

All present enzymatic activity of BMP1 Complexed with A Reverse Hydroxymate - Compound 1:
3.4.24.19;

The structure of BMP1 Complexed with A Reverse Hydroxymate - Compound 1, PDB code: 6btn was solved by R.Gampe, L.Shewchuk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.08 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.690, 90.239, 124.400, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 22.6

The binding sites of Zinc atom in the BMP1 Complexed with A Reverse Hydroxymate - Compound 1 (pdb code 6btn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the BMP1 Complexed with A Reverse Hydroxymate - Compound 1, PDB code: 6btn:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the BMP1 Complexed with A Reverse Hydroxymate - Compound 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of BMP1 Complexed with A Reverse Hydroxymate - Compound 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn302 b:22.1 occ:1.00 O50 A:E8M304 2.0 24.6 1.0 NE2 A:HIS97 2.1 20.4 1.0 NE2 A:HIS93 2.1 21.1 1.0 NE2 A:HIS103 2.1 20.4 1.0 O53 A:E8M304 2.2 24.1 1.0 C49 A:E8M304 2.7 26.8 1.0 N51 A:E8M304 2.8 24.4 1.0 CD2 A:HIS93 2.9 21.1 1.0 CD2 A:HIS103 2.9 20.6 1.0 CD2 A:HIS97 3.0 21.4 1.0 CE1 A:HIS97 3.1 20.7 1.0 CE1 A:HIS93 3.2 21.4 1.0 CE1 A:HIS103 3.2 20.9 1.0 CG A:HIS93 4.1 21.1 1.0 OH A:TYR152 4.1 23.1 1.0 CG A:HIS103 4.1 20.7 1.0 C46 A:E8M304 4.2 28.8 1.0 ND1 A:HIS97 4.2 20.8 1.0 CG A:HIS97 4.2 21.4 1.0 ND1 A:HIS93 4.2 21.2 1.0 ND1 A:HIS103 4.2 20.4 1.0 C20 A:E8M304 4.4 29.8 1.0 CE1 A:TYR152 4.4 23.5 1.0 CZ A:TYR152 4.7 23.5 1.0 CE A:MET150 4.9 21.2 1.0 C18 A:E8M304 4.9 31.6 1.0 OD1 A:ASN128 4.9 27.7 1.0 O A:HOH510 4.9 43.4 1.0

Zinc binding site 2 out of 4 in the BMP1 Complexed with A Reverse Hydroxymate - Compound 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of BMP1 Complexed with A Reverse Hydroxymate - Compound 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn303 b:21.4 occ:0.60 OE2 A:GLU104 2.3 20.9 1.0 O A:ACE-1 2.3 22.9 1.0 OE1 A:GLN192 2.4 26.2 1.0 O A:HOH459 2.4 24.0 1.0 OE1 A:GLU104 2.4 21.1 1.0 O A:HOH467 2.4 21.1 1.0 O A:HOH417 2.4 19.9 1.0 CD A:GLU104 2.7 21.1 1.0 C A:ACE-1 3.4 22.1 1.0 CD A:GLN192 3.4 26.9 1.0 NE2 A:GLN192 3.8 26.0 1.0 N A:ALA1 3.9 21.7 1.0 O A:HOH419 4.0 19.4 1.0 CG A:GLU104 4.2 20.8 1.0 CB A:ASP145 4.2 23.6 1.0 NH1 A:ARG107 4.3 23.2 1.0 O A:HOH435 4.5 28.8 1.0 CH3 A:ACE-1 4.5 21.7 1.0 OD1 A:ASP189 4.6 24.0 1.0 CG A:GLN192 4.7 27.7 1.0 OG A:SER148 4.7 22.0 1.0 OD2 A:ASP145 4.8 24.3 1.0 CD A:ARG107 4.9 22.3 1.0 O A:THR143 4.9 27.4 1.0 CB A:SER148 5.0 22.8 1.0 CB A:GLN192 5.0 27.9 1.0 N A:ASP145 5.0 23.3 1.0 CB A:GLU104 5.0 20.5 1.0

Zinc binding site 3 out of 4 in the BMP1 Complexed with A Reverse Hydroxymate - Compound 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of BMP1 Complexed with A Reverse Hydroxymate - Compound 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:21.9 occ:1.00 NE2 B:HIS93 2.0 19.7 1.0 O B:HOH406 2.1 26.9 1.0 NE2 B:HIS103 2.1 19.4 1.0 NE2 B:HIS97 2.1 19.0 1.0 O B:HOH489 2.5 31.2 1.0 CD2 B:HIS93 3.0 19.8 1.0 CD2 B:HIS103 3.0 19.5 1.0 CE1 B:HIS93 3.0 19.8 1.0 CE1 B:HIS103 3.1 19.5 1.0 CD2 B:HIS97 3.1 19.0 1.0 CE1 B:HIS97 3.1 19.1 1.0 OE2 B:GLU94 4.1 28.1 1.0 ND1 B:HIS93 4.1 20.0 1.0 CG B:HIS93 4.2 20.0 1.0 ND1 B:HIS103 4.2 19.3 1.0 CG B:HIS103 4.2 19.3 1.0 ND1 B:HIS97 4.2 18.9 1.0 CG B:HIS97 4.2 18.8 1.0 O B:HOH443 4.3 29.2 1.0 O B:HOH502 4.4 37.0 1.0 CE B:MET150 4.8 20.3 1.0 O B:HOH509 4.9 32.8 1.0

Zinc binding site 4 out of 4 in the BMP1 Complexed with A Reverse Hydroxymate - Compound 1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of BMP1 Complexed with A Reverse Hydroxymate - Compound 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:22.9 occ:0.60 O B:ACE-1 2.3 24.3 1.0 OE1 B:GLN192 2.3 26.2 1.0 O B:HOH491 2.4 20.3 1.0 O B:HOH450 2.4 18.3 1.0 OE2 B:GLU104 2.4 22.5 1.0 OE1 B:GLU104 2.5 22.7 1.0 O B:HOH424 2.5 19.5 1.0 CD B:GLU104 2.8 22.1 1.0 C B:ACE-1 3.3 23.4 1.0 CD B:GLN192 3.4 26.5 1.0 N B:ALA1 3.8 22.8 1.0 NE2 B:GLN192 3.9 25.8 1.0 O B:HOH428 4.0 21.6 1.0 CB B:ASP145 4.2 23.0 1.0 NH1 B:ARG107 4.2 24.6 1.0 CG B:GLU104 4.3 22.1 1.0 CH3 B:ACE-1 4.5 23.4 1.0 O B:HOH436 4.5 23.0 1.0 OG B:SER148 4.6 21.2 1.0 OD1 B:ASP189 4.7 21.9 1.0 CG B:GLN192 4.7 26.5 1.0 CB B:SER148 4.8 21.8 1.0 OD2 B:ASP145 4.9 22.4 1.0 O B:THR143 4.9 25.8 1.0 N B:ASP145 4.9 23.6 1.0 CB B:GLN192 4.9 26.4 1.0 CD B:ARG107 4.9 22.9 1.0 CE1 B:PHE101 5.0 25.3 1.0

L.S.Kallander, D.Washburn, M.A.Hilfiker, H.S.Eidam, B.G.Lawhorn, J.Prendergast, R.Fox, S.Dowdell, S.Manns, T.Hoang, S.Zhao, G.Ye, M.Hammond, D.A.Holt, T.Roethke, X.Hong, R.A.Reid, R.Gampe, H.Zhang, E.Diaz, A.R.Rendina, A.M.Quinn, B.Willette. Reverse Hydroxamate Inhibitors of Bone Morphogenetic Protein 1. Acs Med Chem Lett V. 9 736 2018.
ISSN: ISSN 1948-5875
PubMed: 30034610
DOI: 10.1021/ACSMEDCHEMLETT.8B00173