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Zinc in PDB 1mr1: Crystal Structure of A SMAD4-Ski Complex

Protein crystallography data

The structure of Crystal Structure of A SMAD4-Ski Complex, PDB code: 1mr1 was solved by J.-W.Wu, A.R.Krawitz, J.Chai, W.Li, F.Zhang, K.Luo, Y.Shi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.85
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 109.800, 109.800, 141.100, 90.00, 90.00, 120.00
R / Rfree (%) 23.1 / 28

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A SMAD4-Ski Complex (pdb code 1mr1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of A SMAD4-Ski Complex, PDB code: 1mr1:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1mr1

Go back to Zinc Binding Sites List in 1mr1
Zinc binding site 1 out of 2 in the Crystal Structure of A SMAD4-Ski Complex


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 A SMAD4-Ski Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn601

b:50.6
occ:1.00
NE2 C:HIS264 1.9 52.4 1.0
SG C:CYS247 2.1 45.7 1.0
NE2 C:HIS262 2.1 46.0 1.0
SG C:CYS250 2.2 51.3 1.0
CD2 C:HIS264 2.8 51.2 1.0
CE1 C:HIS262 2.9 44.6 1.0
CE1 C:HIS264 2.9 51.3 1.0
CB C:CYS247 3.0 45.0 1.0
CD2 C:HIS262 3.2 45.1 1.0
CB C:CYS250 3.3 55.0 1.0
N C:CYS250 3.6 57.8 1.0
OH C:TYR254 3.9 47.3 1.0
ND1 C:HIS264 4.0 50.9 1.0
CG C:HIS264 4.0 50.6 1.0
CA C:CYS250 4.0 55.5 1.0
ND1 C:HIS262 4.1 44.4 1.0
CG C:HIS262 4.2 44.7 1.0
CB C:ASP249 4.3 66.2 1.0
CE1 C:TYR254 4.4 46.5 1.0
CA C:CYS247 4.4 46.6 1.0
CZ C:TYR254 4.4 46.2 1.0
C C:ASP249 4.7 59.7 1.0
SG C:CYS228 4.8 38.1 1.0
C C:CYS250 4.8 56.0 1.0
N C:ASP249 4.9 56.9 1.0
CA C:ASP249 4.9 60.8 1.0
C C:CYS247 4.9 49.0 1.0

Zinc binding site 2 out of 2 in 1mr1

Go back to Zinc Binding Sites List in 1mr1
Zinc binding site 2 out of 2 in the Crystal Structure of A SMAD4-Ski Complex


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 A SMAD4-Ski Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn602

b:52.1
occ:1.00
CE1 D:HIS262 2.0 57.4 1.0
CE1 D:HIS264 2.1 78.6 1.0
SG D:CYS247 2.2 51.7 1.0
SG D:CYS250 2.5 63.3 1.0
ND1 D:HIS264 2.8 78.8 1.0
NE2 D:HIS262 2.8 58.9 1.0
CB D:CYS247 2.8 53.8 1.0
NE2 D:HIS264 3.0 79.7 1.0
ND1 D:HIS262 3.1 57.1 1.0
CB D:CYS250 3.3 62.4 1.0
N D:CYS250 3.5 62.3 1.0
CG D:HIS264 3.8 79.4 1.0
CD2 D:HIS264 3.9 79.3 1.0
CD2 D:HIS262 4.0 59.0 1.0
CA D:CYS250 4.0 62.4 1.0
OH D:TYR254 4.0 49.6 1.0
CG D:HIS262 4.1 58.7 1.0
CE1 D:TYR254 4.3 47.2 1.0
CA D:CYS247 4.3 55.5 1.0
CB D:ASP249 4.4 62.3 1.0
CZ D:TYR254 4.5 48.8 1.0
C D:ASP249 4.6 61.9 1.0
SG D:CYS228 4.6 48.2 1.0
N D:ASP249 4.8 60.4 1.0
CA D:ASP249 4.8 61.1 1.0
C D:CYS247 4.9 55.7 1.0
C D:CYS250 4.9 62.1 1.0
N D:ARG251 5.0 62.3 1.0

Reference:

J.-W.Wu, A.R.Krawitz, J.Chai, W.Li, F.Zhang, K.Luo, Y.Shi. Structural Mechanism of SMAD4 Recognition By the Nuclear Oncoprotein Ski: Insights on Ski-Mediated Repression of Tgf-Beta Signaling Cell(Cambridge,Mass.) V. 111 357 2002.
ISSN: ISSN 0092-8674
PubMed: 12419246
DOI: 10.1016/S0092-8674(02)01006-1
Page generated: Wed Dec 16 02:57:19 2020

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