Zinc in PDB 2lww: uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex

All present enzymatic activity of uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex:
2.3.1.48;

The binding sites of Zinc atom in the uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex (pdb code 2lww). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex, PDB code: 2lww:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:6.0 occ:1.00 NE2 A:HIS362 2.1 6.0 1.0 SG A:CYS379 2.3 6.0 1.0 SG A:CYS384 2.3 6.0 1.0 SG A:CYS366 2.3 6.0 1.0 CE1 A:HIS362 3.0 6.0 1.0 HB2 A:CYS366 3.1 6.0 1.0 CD2 A:HIS362 3.2 6.0 1.0 HE1 A:HIS362 3.2 6.0 1.0 CB A:CYS366 3.2 6.0 1.0 HB3 A:CYS379 3.2 6.0 1.0 CB A:CYS379 3.4 6.0 1.0 HB3 A:CYS366 3.5 6.0 1.0 HD2 A:HIS362 3.5 6.0 1.0 CB A:CYS384 3.6 6.0 1.0 HB2 A:CYS384 3.6 6.0 1.0 HB2 A:CYS379 3.8 6.0 1.0 HB3 A:CYS384 3.9 6.0 1.0 HA A:ALA363 4.0 6.0 1.0 ND1 A:HIS362 4.2 6.0 1.0 CG A:HIS362 4.3 6.0 1.0 CA A:CYS366 4.6 6.0 1.0 CA A:CYS379 4.7 6.0 1.0 H A:CYS379 4.7 6.0 1.0 HA A:CYS379 4.7 6.0 1.0 HA A:CYS366 4.8 6.0 1.0 CA A:CYS384 4.9 6.0 1.0 CA A:ALA363 5.0 6.0 1.0

Zinc binding site 2 out of 3 in the uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:6.0 occ:1.00 NE2 A:HIS393 2.1 6.0 1.0 SG A:CYS408 2.3 6.0 1.0 SG A:CYS403 2.3 6.0 1.0 SG A:CYS397 2.3 6.0 1.0 HH22 A:ARG412 3.0 6.0 1.0 CD2 A:HIS393 3.0 6.0 1.0 CB A:CYS397 3.1 6.0 1.0 HH12 A:ARG412 3.1 6.0 1.0 HB3 A:CYS397 3.1 6.0 1.0 HB2 A:CYS397 3.1 6.0 1.0 HD2 A:HIS393 3.1 6.0 1.0 CE1 A:HIS393 3.2 6.0 1.0 CB A:CYS403 3.3 6.0 1.0 HB2 A:CYS403 3.3 6.0 1.0 CB A:CYS408 3.4 6.0 1.0 HB3 A:CYS403 3.5 6.0 1.0 HE1 A:HIS393 3.5 6.0 1.0 HB2 A:CYS408 3.6 6.0 1.0 HB3 A:CYS408 3.6 6.0 1.0 HB A:VAL405 3.8 6.0 1.0 NH2 A:ARG412 4.0 6.0 1.0 NH1 A:ARG412 4.0 6.0 1.0 CG A:HIS393 4.2 6.0 1.0 ND1 A:HIS393 4.3 6.0 1.0 HG22 A:VAL405 4.3 6.0 1.0 HG21 A:VAL405 4.4 6.0 1.0 HA A:MET394 4.5 6.0 1.0 CZ A:ARG412 4.5 6.0 1.0 CA A:CYS397 4.5 6.0 1.0 HH21 A:ARG412 4.7 6.0 1.0 CA A:CYS403 4.7 6.0 1.0 CB A:VAL405 4.7 6.0 1.0 H A:VAL405 4.7 6.0 1.0 CG2 A:VAL405 4.7 6.0 1.0 HH11 A:ARG412 4.8 6.0 1.0 HA A:CYS403 4.8 6.0 1.0 HA A:CYS397 4.8 6.0 1.0 CA A:CYS408 4.8 6.0 1.0

Zinc binding site 3 out of 3 in the uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of uc(Nmr) Structure of Rela-Tad/Cbp-TAZ1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn503 b:6.0 occ:1.00 NE2 A:HIS417 2.1 6.0 1.0 SG A:CYS421 2.3 6.0 1.0 SG A:CYS426 2.3 6.0 1.0 SG A:CYS429 2.3 6.0 1.0 HB3 A:CYS426 2.9 6.0 1.0 CD2 A:HIS417 3.0 6.0 1.0 CB A:CYS426 3.0 6.0 1.0 HD2 A:HIS417 3.1 6.0 1.0 HB2 A:CYS426 3.1 6.0 1.0 CE1 A:HIS417 3.2 6.0 1.0 CB A:CYS421 3.4 6.0 1.0 HB2 A:CYS421 3.4 6.0 1.0 HE1 A:HIS417 3.6 6.0 1.0 HB3 A:CYS421 3.6 6.0 1.0 CB A:CYS429 3.8 6.0 1.0 HB2 A:CYS429 3.9 6.0 1.0 H A:CYS429 4.1 6.0 1.0 CG A:HIS417 4.2 6.0 1.0 HA A:ARG423 4.2 6.0 1.0 ND1 A:HIS417 4.3 6.0 1.0 HB3 A:CYS429 4.4 6.0 1.0 CA A:CYS426 4.5 6.0 1.0 HB2 B:LEU465 4.5 6.0 1.0 N A:CYS429 4.7 6.0 1.0 HD21 B:LEU465 4.7 6.0 1.0 HB3 A:ARG423 4.8 6.0 1.0 CA A:CYS421 4.8 6.0 1.0 HA A:CYS426 4.8 6.0 1.0 CA A:CYS429 4.9 6.0 1.0 HB A:VAL428 4.9 6.0 1.0 H B:LEU465 4.9 6.0 1.0 HA A:CYS421 5.0 6.0 1.0 H A:VAL428 5.0 6.0 1.0

S.P.Mukherjee, M.Behar, H.A.Birnbaum, A.Hoffmann, P.E.Wright, G.Ghosh. Analysis of the Rela:Cbp/P300 Interaction Reveals Its Involvement in Nf-Kappa B-Driven Transcription. Plos Biol. V. 11 01647 2013.
ISSN: ISSN 1544-9173
PubMed: 24019758
DOI: 10.1371/JOURNAL.PBIO.1001647