Zinc in PDB 7lvs: The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide

All present enzymatic activity of The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide:
2.3.1.48;

The structure of The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide, PDB code: 7lvs was solved by F.D.Appling, R.B.Berlow, R.L.Stanfield, H.J.Dyson, P.E.Wright, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.73 / 2.02
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	32.061, 50.112, 41.255, 90, 99.19, 90
R / Rfree (%)	21.1 / 24.1

The binding sites of Zinc atom in the The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide (pdb code 7lvs). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide, PDB code: 7lvs:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:42.5 occ:0.96 NE2 B:HIS417 2.0 52.0 1.0 SG B:CYS429 2.3 51.5 1.0 SG B:CYS421 2.3 62.5 1.0 SG B:CYS426 2.3 58.4 1.0 CD2 B:HIS417 2.9 40.8 1.0 HB2 B:CYS421 3.0 63.6 1.0 CB B:CYS421 3.0 53.0 1.0 CE1 B:HIS417 3.0 44.4 1.0 HD2 B:HIS417 3.1 49.0 1.0 HB3 B:CYS421 3.1 63.6 1.0 HB2 B:CYS429 3.1 65.9 1.0 HE1 B:HIS417 3.3 53.3 1.0 CB B:CYS426 3.3 68.4 1.0 HB2 B:CYS426 3.3 82.1 1.0 HB3 B:CYS426 3.3 82.1 1.0 CB B:CYS429 3.4 54.9 1.0 H B:CYS429 3.4 51.9 1.0 HB B:VAL428 3.8 61.5 1.0 O B:HOH611 3.9 61.9 1.0 N B:CYS429 4.0 43.2 1.0 HG12 B:VAL428 4.1 53.8 1.0 CG B:HIS417 4.1 43.8 1.0 HB3 B:CYS429 4.1 65.9 1.0 ND1 B:HIS417 4.1 42.8 1.0 CA B:CYS429 4.3 53.6 1.0 HE2 B:LYS433 4.4 83.5 1.0 HD3 B:ARG423 4.5 111.6 1.0 CA B:CYS421 4.5 51.1 1.0 H B:VAL428 4.5 66.3 1.0 CB B:VAL428 4.6 51.2 1.0 HA B:CYS429 4.7 64.4 1.0 CG1 B:VAL428 4.7 44.8 1.0 CA B:CYS426 4.7 72.4 1.0 HA B:CYS421 4.8 61.3 1.0 O B:HIS417 4.8 42.3 1.0 HD1 B:HIS417 4.9 51.4 1.0 C B:VAL428 4.9 49.6 1.0 HG11 B:VAL428 5.0 53.8 1.0 HA B:TRP418 5.0 52.8 1.0

Zinc binding site 2 out of 3 in the The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:43.8 occ:0.63 NE2 B:HIS362 2.0 56.1 1.0 SG B:CYS379 2.3 73.1 1.0 SG B:CYS384 2.3 51.9 1.0 SG B:CYS366 2.3 66.1 1.0 CD2 B:HIS362 2.9 43.0 1.0 HD2 B:HIS362 3.0 51.7 1.0 HB2 B:CYS366 3.1 67.2 1.0 HB2 B:CYS379 3.1 84.6 1.0 CE1 B:HIS362 3.1 50.4 1.0 CB B:CYS379 3.2 70.5 1.0 CB B:CYS366 3.2 56.0 1.0 HB2 B:CYS384 3.3 47.0 1.0 HB3 B:CYS379 3.3 84.6 1.0 CB B:CYS384 3.4 39.1 1.0 HE1 B:HIS362 3.4 60.5 1.0 HB3 B:CYS366 3.5 67.2 1.0 HE3 B:LYS388 3.5 60.8 1.0 HB3 B:CYS384 3.6 47.0 1.0 HB3 B:LEU381 4.0 62.0 1.0 CG B:HIS362 4.1 36.6 1.0 HA B:ALA363 4.1 53.5 1.0 ND1 B:HIS362 4.1 39.5 1.0 HZ1 B:LYS388 4.4 73.5 1.0 CE B:LYS388 4.4 50.6 1.0 HB2 B:LEU381 4.5 62.0 1.0 H B:LEU381 4.6 61.5 1.0 CA B:CYS379 4.6 75.3 1.0 CA B:CYS366 4.7 46.7 1.0 HZ2 B:LYS388 4.7 73.5 1.0 NZ B:LYS388 4.7 61.2 1.0 CA B:CYS384 4.7 43.6 1.0 HE2 B:LYS388 4.7 60.8 1.0 CB B:LEU381 4.7 51.6 1.0 HD23 B:LEU381 4.7 74.0 1.0 HA B:CYS366 4.8 56.0 1.0 HA B:CYS379 4.8 90.5 1.0 HD22 B:LEU381 4.8 74.0 1.0 HA B:CYS384 4.8 52.4 1.0 HD1 B:HIS362 4.9 47.5 1.0

Zinc binding site 3 out of 3 in the The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Cbp TAZ1 Domain in Complex with A CITED2-Hif-1-Alpha Fusion Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn503 b:42.1 occ:0.81 NE2 B:HIS393 2.0 49.4 1.0 SG B:CYS403 2.3 59.8 1.0 SG B:CYS397 2.3 57.9 1.0 SG B:CYS408 2.3 42.7 1.0 HB2 B:CYS397 2.9 77.2 1.0 CD2 B:HIS393 2.9 47.0 1.0 HD2 B:HIS393 3.0 56.4 1.0 CE1 B:HIS393 3.1 49.7 1.0 CB B:CYS397 3.1 64.3 1.0 HE1 B:HIS393 3.3 59.7 1.0 HB2 B:CYS403 3.4 78.4 1.0 CB B:CYS408 3.4 31.0 1.0 CB B:CYS403 3.4 65.3 1.0 HB3 B:CYS408 3.4 37.3 1.0 HB2 B:CYS408 3.4 37.3 1.0 HB3 B:CYS397 3.5 77.2 1.0 HB3 B:CYS403 3.6 78.4 1.0 HB B:VAL405 3.9 68.7 1.0 O B:HOH601 4.0 54.8 1.0 CG B:HIS393 4.1 48.2 1.0 ND1 B:HIS393 4.1 41.7 1.0 HH21 B:ARG412 4.1 48.9 1.0 HB3 B:ALA399 4.1 78.5 1.0 HA B:MET394 4.3 51.9 1.0 CA B:CYS397 4.5 57.7 1.0 HG3 B:MET394 4.6 45.7 1.0 HA B:CYS397 4.6 69.3 1.0 H B:ALA399 4.6 79.8 1.0 H B:VAL405 4.7 78.8 1.0 CA B:CYS403 4.8 63.0 1.0 CA B:CYS408 4.8 31.0 1.0 NH2 B:ARG412 4.8 40.8 1.0 CB B:VAL405 4.8 57.2 1.0 HD1 B:HIS393 4.9 50.1 1.0 HH22 B:ARG412 4.9 48.9 1.0 HA B:CYS403 4.9 75.6 1.0 HG21 B:VAL405 5.0 70.4 1.0

F.D.Appling, R.B.Berlow, R.L.Stanfield, H.J.Dyson, P.E.Wright. The Molecular Basis of Allostery in A Facilitated Dissociation Reaction To Be Published.