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Zinc in PDB 1j2x: Crystal Structure of RAP74 C-Terminal Domain Complexed with FCP1 C-Terminal Peptide

Protein crystallography data

The structure of Crystal Structure of RAP74 C-Terminal Domain Complexed with FCP1 C-Terminal Peptide, PDB code: 1j2x was solved by K.Kamada, R.G.Roeder, S.K.Burley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.73 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 59.605, 30.446, 47.379, 90.00, 106.38, 90.00
R / Rfree (%) 20.3 / 25.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of RAP74 C-Terminal Domain Complexed with FCP1 C-Terminal Peptide (pdb code 1j2x). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of RAP74 C-Terminal Domain Complexed with FCP1 C-Terminal Peptide, PDB code: 1j2x:

Zinc binding site 1 out of 1 in 1j2x

Go back to Zinc Binding Sites List in 1j2x
Zinc binding site 1 out of 1 in the Crystal Structure of RAP74 C-Terminal Domain Complexed with FCP1 C-Terminal 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 RAP74 C-Terminal Domain Complexed with FCP1 C-Terminal Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1000

b:16.9
occ:1.00
OE1 A:GLU503 2.0 23.6 1.0
O A:GLU517 2.1 23.5 1.0
OE2 A:GLU503 2.3 20.2 1.0
CD A:GLU503 2.4 21.4 1.0
C A:GLU517 2.9 28.9 1.0
OXT A:GLU517 3.1 28.3 1.0
O A:HOH1012 3.6 26.8 1.0
CG A:GLU503 3.9 21.9 1.0
CA A:GLU517 4.3 30.0 1.0
CE A:LYS505 4.5 33.9 1.0
O A:HOH1022 4.5 27.4 1.0
NZ A:LYS505 4.6 33.7 1.0
O A:LYS516 4.7 23.8 1.0
CB A:GLU503 4.8 20.4 1.0

Reference:

K.Kamada, R.G.Roeder, S.K.Burley. Molecular Mechanism of Recruitment of Tfiif- Associating Rna Polymerase C-Terminal Domain Phosphatase (FCP1) By Transcription Factor Iif Proc.Natl.Acad.Sci.Usa V. 100 2296 2003.
ISSN: ISSN 0027-8424
PubMed: 12591941
DOI: 10.1073/PNAS.262798199
Page generated: Fri Sep 25 22:05:20 2020
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