Zinc in PDB 2jmi: uc(Nmr) Solution Structure of Phd Finger Fragment of Yeast YNG1 Protein in Free State

The binding sites of Zinc atom in the uc(Nmr) Solution Structure of Phd Finger Fragment of Yeast YNG1 Protein in Free State (pdb code 2jmi). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the uc(Nmr) Solution Structure of Phd Finger Fragment of Yeast YNG1 Protein in Free State, PDB code: 2jmi:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the uc(Nmr) Solution Structure of Phd Finger Fragment of Yeast YNG1 Protein in Free State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Solution Structure of Phd Finger Fragment of Yeast YNG1 Protein in Free State within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:12.5 occ:1.00 SG A:CYS73 1.3 12.5 1.0 SG A:CYS42 1.4 12.5 1.0 SG A:CYS69 1.5 100.0 1.0 SG A:CYS47 1.6 12.5 1.0 HB2 A:CYS69 2.3 0.0 1.0 CB A:CYS69 2.4 100.0 1.0 CB A:CYS73 2.6 12.5 1.0 CB A:CYS47 2.6 12.5 1.0 HB2 A:CYS73 2.6 0.0 1.0 HA A:CYS47 2.6 0.0 1.0 HB3 A:CYS47 2.7 0.0 1.0 CB A:CYS42 2.8 12.5 1.0 HB2 A:CYS42 2.8 0.0 1.0 HB3 A:CYS69 2.9 0.0 1.0 CA A:CYS47 3.1 12.5 1.0 HB3 A:CYS42 3.3 0.0 1.0 HD2 A:PRO48 3.3 0.0 1.0 HB3 A:CYS73 3.3 0.0 1.0 HA A:CYS73 3.4 0.0 1.0 HZ A:PHE52 3.5 0.0 1.0 HB2 A:CYS47 3.5 0.0 1.0 CA A:CYS73 3.6 12.5 1.0 CA A:CYS69 3.7 100.0 1.0 H A:PHE49 3.8 0.0 1.0 CZ A:PHE52 3.8 12.5 1.0 HA A:CYS42 3.8 0.0 1.0 C A:CYS47 3.9 12.5 1.0 H A:CYS69 3.9 0.0 1.0 CA A:CYS42 3.9 12.5 1.0 HE1 A:PHE52 4.0 0.0 1.0 H A:SER70 4.0 0.0 1.0 O A:PHE49 4.0 12.5 1.0 CE1 A:PHE52 4.0 12.5 1.0 N A:CYS69 4.1 100.0 1.0 CD A:PRO48 4.2 25.0 1.0 C A:CYS69 4.3 100.0 1.0 N A:PRO48 4.3 12.5 1.0 N A:CYS47 4.3 12.5 1.0 N A:SER70 4.3 100.0 1.0 HB3 A:ASN44 4.4 0.0 1.0 CE2 A:PHE52 4.5 12.5 1.0 HA A:CYS69 4.5 0.0 1.0 HB2 A:SER70 4.5 0.0 1.0 H A:CYS47 4.5 0.0 1.0 H A:CYS73 4.5 0.0 1.0 N A:CYS73 4.6 12.5 1.0 C A:CYS73 4.6 12.5 1.0 O A:CYS47 4.6 12.5 1.0 HG2 A:PRO48 4.7 0.0 1.0 O A:CYS73 4.7 12.5 1.0 N A:PHE49 4.7 12.5 1.0 HE2 A:PHE52 4.8 0.0 1.0 HD13 A:ILE76 4.8 0.0 1.0 OD1 A:ASN44 4.8 12.5 1.0 CD1 A:PHE52 4.9 12.5 1.0 C A:PHE49 4.9 12.5 1.0 C A:CYS42 4.9 12.5 1.0 H A:CYS42 4.9 0.0 1.0 N A:CYS42 4.9 12.5 1.0 HD3 A:PRO48 4.9 0.0 1.0

Zinc binding site 2 out of 2 in the uc(Nmr) Solution Structure of Phd Finger Fragment of Yeast YNG1 Protein in Free State


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of uc(Nmr) Solution Structure of Phd Finger Fragment of Yeast YNG1 Protein in Free State within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:12.5 occ:1.00 SG A:CYS56 1.3 12.5 1.0 SG A:CYS31 1.4 12.5 1.0 SG A:CYS29 1.6 12.5 1.0 CB A:CYS56 2.4 12.5 1.0 HB3 A:CYS56 2.5 0.0 1.0 CB A:CYS31 2.6 12.5 1.0 H A:CYS31 2.6 0.0 1.0 HB3 A:CYS31 2.7 0.0 1.0 HB2 A:CYS29 2.7 0.0 1.0 CB A:CYS29 2.7 12.5 1.0 N A:CYS31 2.9 12.5 1.0 HA A:CYS56 3.0 0.0 1.0 CA A:CYS56 3.2 12.5 1.0 CA A:CYS31 3.2 12.5 1.0 HB2 A:CYS56 3.3 0.0 1.0 H A:PHE30 3.4 0.0 1.0 N A:PHE30 3.4 12.5 1.0 HB2 A:CYS31 3.5 0.0 1.0 HB3 A:CYS29 3.5 0.0 1.0 HD1 A:HIS53 3.5 0.0 1.0 C A:CYS29 3.5 12.5 1.0 C A:PHE30 3.6 12.5 1.0 HD22 A:ASN33 3.6 0.0 1.0 CA A:CYS29 3.7 12.5 1.0 C A:CYS56 3.7 12.5 1.0 HA A:CYS31 3.7 0.0 1.0 O A:CYS56 3.9 12.5 1.0 CA A:PHE30 4.1 12.5 1.0 HE1 A:HIS53 4.1 0.0 1.0 O A:CYS29 4.1 12.5 1.0 ND1 A:HIS53 4.1 12.5 1.0 HA A:CYS29 4.2 0.0 1.0 HB2 A:PHE30 4.2 0.0 1.0 HG12 A:VAL57 4.3 0.0 1.0 O A:PHE30 4.4 12.5 1.0 ND2 A:ASN33 4.4 50.0 1.0 HD2 A:PHE52 4.4 0.0 1.0 CE1 A:HIS53 4.4 12.5 1.0 H A:HIS53 4.5 0.0 1.0 N A:CYS56 4.5 12.5 1.0 C A:CYS31 4.5 12.5 1.0 HD21 A:ASN33 4.6 0.0 1.0 N A:VAL57 4.6 12.5 1.0 CB A:PHE30 4.8 16.7 1.0 H A:ARG32 4.8 0.0 1.0 H A:CYS56 4.8 0.0 1.0 H A:VAL57 4.8 0.0 1.0 N A:CYS29 4.9 12.5 1.0 HB3 A:PHE52 4.9 0.0 1.0 HA A:PHE30 5.0 0.0 1.0

S.D.Taverna, S.Ilin, R.S.Rogers, J.C.Tanny, H.Lavender, H.Li, L.Baker, J.Boyle, L.P.Blair, B.T.Chait, D.J.Patel, J.D.Aitchison, A.J.Tackett, C.D.Allis. YNG1 Phd Finger Binding to H3 Trimethylated at K4 Promotes NUA3 Hat Activity at K14 of H3 and Transcription at A Subset of Targeted Orfs Mol.Cell V. 24 785 2006.
ISSN: ISSN 1097-2765
PubMed: 17157260
DOI: 10.1016/J.MOLCEL.2006.10.026