Zinc in PDB 4xxb: Crystal Structure of Human MDM2-RPL11

The structure of Crystal Structure of Human MDM2-RPL11, PDB code: 4xxb was solved by J.Zheng, Z.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.40
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	58.307, 58.307, 115.129, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 22.7

The binding sites of Zinc atom in the Crystal Structure of Human MDM2-RPL11 (pdb code 4xxb). 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 Human MDM2-RPL11, PDB code: 4xxb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human MDM2-RPL11


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 Human MDM2-RPL11 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn203 b:48.9 occ:1.00 N3 A:IMD201 2.0 47.7 1.0 NE2 B:HIS318 2.1 44.9 1.0 O A:HOH322 2.3 22.4 1.0 SG A:CYS25 2.4 47.4 1.0 CE1 B:HIS318 2.8 45.8 1.0 C4 A:IMD201 3.0 49.3 1.0 CB A:CYS25 3.1 44.4 1.0 C2 A:IMD201 3.1 50.4 1.0 CD2 B:HIS318 3.2 42.5 1.0 CA A:CYS25 4.0 42.1 1.0 CB B:PRO316 4.0 45.7 1.0 ND1 B:HIS318 4.1 44.3 1.0 O B:HOH627 4.1 55.2 1.0 C5 A:IMD201 4.2 49.5 1.0 N1 A:IMD201 4.2 48.8 1.0 CZ2 B:TRP323 4.2 45.2 1.0 CG B:HIS318 4.3 43.0 1.0 CG B:PRO316 4.3 46.0 1.0 CB A:ALA69 4.4 36.6 1.0 CD1 A:ILE68 4.6 40.7 1.0 CH2 B:TRP323 4.7 43.6 1.0 C A:CYS25 4.9 42.3 1.0 CE2 B:TRP323 4.9 43.9 1.0 O A:ILE68 4.9 39.2 1.0 N A:VAL26 5.0 43.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human MDM2-RPL11


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 Human MDM2-RPL11 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:40.5 occ:1.00 SG B:CYS322 2.2 40.8 1.0 SG B:CYS319 2.3 39.3 1.0 SG B:CYS305 2.4 44.3 1.0 SG B:CYS308 2.5 40.7 1.0 CB B:CYS319 3.0 41.1 1.0 CB B:CYS305 3.3 44.7 1.0 CB B:CYS308 3.3 40.0 1.0 CB B:CYS322 3.3 40.6 1.0 N B:CYS322 3.8 42.1 1.0 N B:CYS308 4.0 43.5 1.0 CA B:CYS322 4.1 40.0 1.0 CA B:CYS308 4.1 43.4 1.0 CA B:CYS319 4.5 40.0 1.0 CB B:ARG321 4.6 43.6 1.0 CB B:GLU310 4.6 44.6 1.0 CB B:SER307 4.6 46.9 1.0 CB B:ALA324 4.6 36.8 1.0 C B:CYS322 4.7 42.4 1.0 C B:CYS308 4.7 47.1 1.0 C B:SER307 4.7 46.5 1.0 CA B:CYS305 4.7 45.3 1.0 C B:ARG321 4.8 42.9 1.0 N B:TRP323 4.8 42.0 1.0 N B:ASN309 4.9 44.5 1.0 N B:ALA324 4.9 40.4 1.0 N B:GLU310 4.9 44.7 1.0

J.Zheng, Y.Lang, Q.Zhang, D.Cui, H.Sun, L.Jiang, Z.Chen, R.Zhang, Y.Gao, W.Tian, W.Wu, J.Tang, Z.Chen. Structure of Human MDM2 Complexed with RPL11 Reveals the Molecular Basis of P53 Activation Genes Dev. V. 29 1524 2015.
ISSN: ISSN 0890-9369
PubMed: 26220995
DOI: 10.1101/GAD.261792.115