Zinc in PDB 4q6f: Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide

The structure of Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide, PDB code: 4q6f was solved by C.Tallant, L.Overvoorde, T.Krojer, P.Filippakopoulos, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, C.Bountra, A.Ciulli, S.Knapp, Structuralgenomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.06 / 1.91
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	71.866, 71.866, 98.767, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21.9

The binding sites of Zinc atom in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide (pdb code 4q6f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide, PDB code: 4q6f:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1801 b:26.1 occ:1.00 ND1 A:HIS1702 2.1 25.3 1.0 SG A:CYS1705 2.3 24.5 1.0 SG A:CYS1682 2.4 29.1 1.0 SG A:CYS1679 2.4 26.1 1.0 CB A:CYS1679 3.0 26.6 1.0 CE1 A:HIS1702 3.0 26.6 1.0 CG A:HIS1702 3.1 23.6 1.0 CB A:CYS1682 3.2 29.2 1.0 CB A:CYS1705 3.3 22.7 1.0 CB A:HIS1702 3.4 22.4 1.0 N A:CYS1682 3.8 29.7 1.0 CA A:CYS1682 4.1 31.6 1.0 N A:HIS1702 4.1 21.0 1.0 NE2 A:HIS1702 4.2 25.9 1.0 CD2 A:HIS1702 4.2 24.4 1.0 O A:HOH1913 4.3 42.4 1.0 CE1 A:TYR1704 4.3 24.1 1.0 CA A:HIS1702 4.4 22.3 1.0 CA A:CYS1679 4.5 28.3 1.0 CB A:VAL1681 4.6 29.0 1.0 CA A:CYS1705 4.7 21.7 1.0 C A:CYS1682 4.8 31.5 1.0 C A:VAL1681 4.9 32.3 1.0 CD1 A:TYR1704 4.9 22.9 1.0 N A:ARG1683 5.0 34.0 1.0 N A:CYS1705 5.0 20.6 1.0 CZ A:TYR1704 5.0 26.9 1.0

Zinc binding site 2 out of 8 in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1802 b:28.4 occ:1.00 SG A:CYS1697 2.2 31.4 1.0 SG A:CYS1694 2.2 28.6 1.0 SG A:CYS1720 2.3 28.0 1.0 SG A:CYS1723 2.4 30.4 1.0 CB A:CYS1694 3.2 29.2 1.0 CB A:CYS1697 3.3 34.3 1.0 CB A:CYS1720 3.4 28.3 1.0 CB A:CYS1723 3.4 28.4 1.0 N A:CYS1697 3.7 34.8 1.0 N A:CYS1720 3.9 26.3 1.0 N A:CYS1723 3.9 28.1 1.0 CA A:CYS1697 4.0 34.5 1.0 CA A:CYS1720 4.1 26.9 1.0 C A:GLY1696 4.1 37.6 1.0 CA A:CYS1723 4.2 28.0 1.0 CA A:GLY1696 4.5 36.1 1.0 N A:GLY1696 4.6 36.1 1.0 NH1 A:ARG1699 4.6 35.9 1.0 C A:CYS1720 4.7 28.2 1.0 CA A:CYS1694 4.7 29.3 1.0 C A:CYS1697 4.7 34.5 1.0 CB A:ARG1699 4.7 34.0 1.0 CD A:ARG1699 4.7 35.4 1.0 O A:CYS1720 4.7 25.4 1.0 O A:GLY1696 4.7 37.4 1.0 CG A:ARG1699 4.9 34.8 1.0 CB A:VAL1722 5.0 32.8 1.0 C A:PHE1719 5.0 27.3 1.0 C A:VAL1722 5.0 29.7 1.0

Zinc binding site 3 out of 8 in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1801 b:26.2 occ:1.00 ND1 B:HIS1702 2.0 25.5 1.0 SG B:CYS1682 2.2 27.6 1.0 SG B:CYS1705 2.3 26.6 1.0 SG B:CYS1679 2.4 24.1 1.0 CE1 B:HIS1702 2.9 27.0 1.0 CB B:CYS1679 3.1 25.6 1.0 CG B:HIS1702 3.1 24.4 1.0 CB B:CYS1682 3.3 26.9 1.0 CB B:CYS1705 3.4 24.9 1.0 CB B:HIS1702 3.5 24.1 1.0 N B:CYS1682 3.7 27.6 1.0 N B:HIS1702 4.0 24.0 1.0 CA B:CYS1682 4.0 29.8 1.0 NE2 B:HIS1702 4.1 26.1 1.0 CD2 B:HIS1702 4.2 26.2 1.0 CA B:HIS1702 4.4 23.5 1.0 CE1 B:TYR1704 4.4 26.1 1.0 CA B:CYS1679 4.5 26.8 1.0 O B:HOH1910 4.6 36.3 1.0 CB B:VAL1681 4.7 26.6 1.0 CA B:CYS1705 4.8 26.9 1.0 C B:VAL1681 4.8 28.2 1.0 C B:CYS1682 4.9 31.0 1.0 CZ B:TYR1704 4.9 25.0 1.0 OH B:TYR1704 4.9 27.4 1.0

Zinc binding site 4 out of 8 in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1802 b:24.1 occ:1.00 SG B:CYS1694 2.2 25.7 1.0 SG B:CYS1697 2.3 25.6 1.0 SG B:CYS1720 2.4 22.1 1.0 SG B:CYS1723 2.4 25.5 1.0 CB B:CYS1694 3.2 26.0 1.0 CB B:CYS1723 3.3 23.9 1.0 CB B:CYS1697 3.4 27.1 1.0 CB B:CYS1720 3.5 22.2 1.0 N B:CYS1697 3.7 26.6 1.0 N B:CYS1720 3.9 22.3 1.0 N B:CYS1723 4.0 22.6 1.0 CA B:CYS1697 4.1 26.9 1.0 C B:GLY1696 4.1 29.4 1.0 CA B:CYS1720 4.2 23.0 1.0 CA B:CYS1723 4.3 23.8 1.0 CA B:GLY1696 4.5 27.6 1.0 N B:GLY1696 4.6 29.8 1.0 CA B:CYS1694 4.6 27.5 1.0 C B:CYS1697 4.7 28.2 1.0 C B:CYS1720 4.7 23.4 1.0 O B:CYS1720 4.7 20.5 1.0 CB B:ARG1699 4.7 25.2 1.0 NH1 B:ARG1699 4.8 25.8 1.0 O B:GLY1696 4.8 27.1 1.0 CB B:VAL1722 4.9 24.8 1.0 CD B:ARG1699 4.9 24.5 1.0 O B:CYS1697 4.9 27.5 1.0

Zinc binding site 5 out of 8 in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1800 b:32.5 occ:1.00 ND1 C:HIS1702 2.0 28.4 1.0 SG C:CYS1705 2.3 29.9 1.0 SG C:CYS1679 2.3 31.9 1.0 SG C:CYS1682 2.4 36.0 1.0 CE1 C:HIS1702 3.0 32.4 1.0 CG C:HIS1702 3.0 28.0 1.0 CB C:CYS1679 3.1 35.8 1.0 CB C:CYS1682 3.2 36.8 1.0 CB C:CYS1705 3.3 28.5 1.0 CB C:HIS1702 3.4 25.4 1.0 N C:CYS1682 3.8 36.8 1.0 NE2 C:HIS1702 4.1 29.9 1.0 CA C:CYS1682 4.1 40.9 1.0 N C:HIS1702 4.1 25.0 1.0 CD2 C:HIS1702 4.1 27.6 1.0 CA C:HIS1702 4.4 25.0 1.0 CE1 C:TYR1704 4.4 32.7 1.0 CA C:CYS1679 4.6 37.8 1.0 CA C:CYS1705 4.7 28.2 1.0 CB C:VAL1681 4.7 34.5 1.0 C C:VAL1681 4.9 37.1 1.0 N C:CYS1705 4.9 26.5 1.0 C C:CYS1682 4.9 43.8 1.0 N C:VAL1681 4.9 32.9 1.0 CD1 C:TYR1704 5.0 33.5 1.0

Zinc binding site 6 out of 8 in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1801 b:35.9 occ:1.00 SG C:CYS1697 2.2 38.9 1.0 SG C:CYS1694 2.4 36.1 1.0 SG C:CYS1723 2.4 39.8 1.0 SG C:CYS1720 2.4 32.4 1.0 CB C:CYS1694 3.3 35.6 1.0 CB C:CYS1697 3.3 41.9 1.0 CB C:CYS1720 3.4 31.7 1.0 CB C:CYS1723 3.5 40.4 1.0 N C:CYS1697 3.7 44.1 1.0 N C:CYS1720 3.9 31.8 1.0 N C:CYS1723 4.0 42.1 1.0 CA C:CYS1697 4.0 42.0 1.0 CA C:CYS1720 4.1 31.6 1.0 C C:GLY1696 4.2 45.6 1.0 CA C:CYS1723 4.3 41.6 1.0 CA C:GLY1696 4.4 44.3 1.0 O C:CYS1720 4.6 31.2 1.0 N C:GLY1696 4.6 40.6 1.0 C C:CYS1720 4.6 31.5 1.0 CB C:ARG1699 4.7 42.2 1.0 C C:CYS1697 4.7 44.9 1.0 CA C:CYS1694 4.7 35.7 1.0 NH1 C:ARG1699 4.8 48.7 1.0 CD C:ARG1699 4.9 48.6 1.0 O C:CYS1697 5.0 45.7 1.0 O C:GLY1696 5.0 44.4 1.0 CB C:VAL1722 5.0 44.6 1.0 C C:PHE1719 5.0 35.7 1.0

Zinc binding site 7 out of 8 in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1801 b:23.1 occ:1.00 ND1 D:HIS1702 2.0 23.5 1.0 SG D:CYS1705 2.3 22.6 1.0 SG D:CYS1682 2.3 24.9 1.0 SG D:CYS1679 2.3 21.6 1.0 CE1 D:HIS1702 2.9 23.9 1.0 CB D:CYS1679 3.0 21.1 1.0 CG D:HIS1702 3.1 22.4 1.0 CB D:CYS1682 3.2 25.1 1.0 CB D:CYS1705 3.3 22.3 1.0 CB D:HIS1702 3.5 21.7 1.0 N D:CYS1682 3.8 23.8 1.0 NE2 D:HIS1702 4.1 22.5 1.0 N D:HIS1702 4.1 20.2 1.0 CA D:CYS1682 4.1 26.0 1.0 CD2 D:HIS1702 4.2 22.5 1.0 CA D:HIS1702 4.4 21.5 1.0 CA D:CYS1679 4.5 21.7 1.0 CE1 D:TYR1704 4.5 22.6 1.0 CA D:CYS1705 4.7 21.4 1.0 O D:HOH1906 4.7 31.5 1.0 CB D:VAL1681 4.8 22.4 1.0 C D:CYS1682 4.9 26.3 1.0 C D:VAL1681 4.9 25.1 1.0 N D:CYS1705 4.9 20.6 1.0

Zinc binding site 8 out of 8 in the Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Crystal Structure of Human BAZ2A Phd Zinc Finger in Complex with Unmodified H3K4 Histone Peptide within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1802 b:21.6 occ:1.00 SG D:CYS1697 2.3 22.8 1.0 SG D:CYS1694 2.3 23.7 1.0 SG D:CYS1723 2.3 23.6 1.0 SG D:CYS1720 2.3 22.4 1.0 CB D:CYS1723 3.3 24.1 1.0 CB D:CYS1694 3.3 23.3 1.0 CB D:CYS1697 3.3 25.4 1.0 CB D:CYS1720 3.4 23.0 1.0 N D:CYS1697 3.8 26.8 1.0 N D:CYS1720 3.9 25.7 1.0 N D:CYS1723 3.9 21.0 1.0 CA D:CYS1697 4.1 26.5 1.0 CA D:CYS1720 4.2 23.1 1.0 CA D:CYS1723 4.2 23.2 1.0 C D:GLY1696 4.3 27.8 1.0 CA D:GLY1696 4.5 28.0 1.0 N D:GLY1696 4.5 26.4 1.0 NH1 D:ARG1699 4.6 23.1 1.0 O D:CYS1720 4.7 21.4 1.0 C D:CYS1720 4.7 22.7 1.0 C D:CYS1697 4.7 27.1 1.0 CA D:CYS1694 4.7 23.8 1.0 CB D:ARG1699 4.7 21.7 1.0 CD D:ARG1699 4.8 22.1 1.0 O D:GLY1696 4.9 27.6 1.0 O D:CYS1697 5.0 25.7 1.0 C D:PHE1719 5.0 31.0 1.0

C.Tallant, L.Overvoorde, T.Krojer, P.Filippakopoulos, M.Vondelft, C.H.Arrowsmith, A.M.Edwards, C.Bountra, A.Ciulli, S.Knapp. Crystal Structure of BAZ2A Phd Zinc Finger Complexed with Unmodified H3K4 Peptide To Be Published.