Zinc in PDB 5hou: Solution Structure of P53TAD-TAZ1

All present enzymatic activity of Solution Structure of P53TAD-TAZ1:
2.3.1.48;

The binding sites of Zinc atom in the Solution Structure of P53TAD-TAZ1 (pdb code 5hou). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Solution Structure of P53TAD-TAZ1, PDB code: 5hou:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Solution Structure of P53TAD-TAZ1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of P53TAD-TAZ1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn5001 b:0.0 occ:1.00 NE2 A:HIS3362 2.1 0.0 1.0 SG A:CYS3379 2.3 0.0 1.0 SG A:CYS3366 2.3 0.0 1.0 SG A:CYS3384 2.3 0.0 1.0 HB2 A:CYS3379 2.6 0.0 1.0 CD2 A:HIS3362 2.9 0.0 1.0 HB2 A:CYS3366 3.0 0.0 1.0 CB A:CYS3379 3.0 0.0 1.0 HD2 A:HIS3362 3.0 0.0 1.0 CB A:CYS3366 3.1 0.0 1.0 CE1 A:HIS3362 3.2 0.0 1.0 HB3 A:CYS3366 3.3 0.0 1.0 H A:CYS3379 3.5 0.0 1.0 HZ1 A:LYS3388 3.5 0.0 1.0 HB3 A:CYS3379 3.5 0.0 1.0 CB A:CYS3384 3.6 0.0 1.0 HE1 A:HIS3362 3.6 0.0 1.0 HB2 A:CYS3384 3.6 0.0 1.0 HB3 A:CYS3384 3.9 0.0 1.0 CG A:HIS3362 4.1 0.0 1.0 HD22 A:LEU3381 4.2 0.0 1.0 CA A:CYS3379 4.2 0.0 1.0 N A:CYS3379 4.3 0.0 1.0 ND1 A:HIS3362 4.3 0.0 1.0 NZ A:LYS3388 4.5 0.0 1.0 HA A:ALA3363 4.5 0.0 1.0 HB3 A:LEU3381 4.5 0.0 1.0 CA A:CYS3366 4.5 0.0 1.0 HE3 A:LYS3388 4.6 0.0 1.0 HA A:CYS3379 4.7 0.0 1.0 HE2 A:LYS3388 4.7 0.0 1.0 HA A:CYS3366 4.7 0.0 1.0 CE A:LYS3388 4.9 0.0 1.0 HB3 A:ALA3378 4.9 0.0 1.0 CA A:CYS3384 4.9 0.0 1.0 O A:HIS3362 4.9 0.0 1.0 HZ2 A:LYS3388 5.0 0.0 1.0

Zinc binding site 2 out of 3 in the Solution Structure of P53TAD-TAZ1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of P53TAD-TAZ1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn5002 b:0.0 occ:1.00 NE2 A:HIS3393 2.1 0.0 1.0 SG A:CYS3397 2.3 0.0 1.0 SG A:CYS3408 2.3 0.0 1.0 SG A:CYS3403 2.3 0.0 1.0 CD2 A:HIS3393 2.9 0.0 1.0 HD2 A:HIS3393 2.9 0.0 1.0 HB2 A:CYS3397 3.0 0.0 1.0 HB2 A:CYS3403 3.0 0.0 1.0 CB A:CYS3403 3.1 0.0 1.0 CB A:CYS3397 3.2 0.0 1.0 CE1 A:HIS3393 3.3 0.0 1.0 CB A:CYS3408 3.3 0.0 1.0 HB3 A:CYS3403 3.4 0.0 1.0 HB3 A:CYS3408 3.4 0.0 1.0 HB2 A:CYS3408 3.5 0.0 1.0 HE1 A:HIS3393 3.7 0.0 1.0 HB3 A:CYS3397 3.7 0.0 1.0 CG A:HIS3393 4.1 0.0 1.0 HB A:VAL3405 4.1 0.0 1.0 H A:GLY3400 4.3 0.0 1.0 ND1 A:HIS3393 4.3 0.0 1.0 HA A:MET3394 4.3 0.0 1.0 HA A:CYS3397 4.5 0.0 1.0 CA A:CYS3397 4.5 0.0 1.0 HB1 A:ALA3399 4.5 0.0 1.0 CA A:CYS3403 4.5 0.0 1.0 HA A:CYS3403 4.7 0.0 1.0 H A:ALA3399 4.7 0.0 1.0 CA A:CYS3408 4.7 0.0 1.0 H A:VAL3405 4.8 0.0 1.0 HA2 A:GLY3400 4.8 0.0 1.0 N A:GLY3400 5.0 0.0 1.0

Zinc binding site 3 out of 3 in the Solution Structure of P53TAD-TAZ1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Solution Structure of P53TAD-TAZ1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn5003 b:0.0 occ:1.00 NE2 A:HIS3417 2.1 0.0 1.0 SG A:CYS3429 2.3 0.0 1.0 SG A:CYS3426 2.3 0.0 1.0 SG A:CYS3421 2.3 0.0 1.0 CE1 A:HIS3417 2.8 0.0 1.0 HE1 A:HIS3417 2.8 0.0 1.0 HB3 A:CYS3421 3.1 0.0 1.0 CB A:CYS3421 3.1 0.0 1.0 CB A:CYS3426 3.2 0.0 1.0 H A:CYS3429 3.2 0.0 1.0 HB3 A:CYS3426 3.2 0.0 1.0 HB2 A:CYS3421 3.3 0.0 1.0 CD2 A:HIS3417 3.3 0.0 1.0 HB2 A:CYS3426 3.4 0.0 1.0 HB A:VAL3428 3.7 0.0 1.0 HD2 A:HIS3417 3.8 0.0 1.0 CB A:CYS3429 3.8 0.0 1.0 HB2 A:CYS3429 4.0 0.0 1.0 ND1 A:HIS3417 4.1 0.0 1.0 N A:CYS3429 4.1 0.0 1.0 CG A:HIS3417 4.3 0.0 1.0 H A:VAL3428 4.4 0.0 1.0 CA A:CYS3429 4.5 0.0 1.0 CA A:CYS3421 4.6 0.0 1.0 HB3 A:CYS3429 4.6 0.0 1.0 HB2 A:ARG3423 4.7 0.0 1.0 CA A:CYS3426 4.7 0.0 1.0 CB A:VAL3428 4.8 0.0 1.0 HD1 A:HIS3417 4.9 0.0 1.0 HA A:CYS3421 4.9 0.0 1.0 HA A:CYS3429 4.9 0.0 1.0 H A:ARG3423 4.9 0.0 1.0

A.S.Krois, J.C.Ferreon, M.A.Martinez-Yamout, H.J.Dyson, P.E.Wright. Recognition of the Disordered P53 Transactivation Domain By the Transcriptional Adapter Zinc Finger Domains of Creb-Binding Protein. Proc.Natl.Acad.Sci.Usa V. 113 E1853 2016.
ISSN: ESSN 1091-6490
PubMed: 26976603
DOI: 10.1073/PNAS.1602487113