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Zinc in PDB 3kyc: Human Sumo E1 Complex with A SUMO1-Amp Mimic

Protein crystallography data

The structure of Human Sumo E1 Complex with A SUMO1-Amp Mimic, PDB code: 3kyc was solved by C.D.Lima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.174, 133.365, 159.656, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 25

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Sumo E1 Complex with A SUMO1-Amp Mimic (pdb code 3kyc). 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 Human Sumo E1 Complex with A SUMO1-Amp Mimic, PDB code: 3kyc:

Zinc binding site 1 out of 1 in 3kyc

Go back to Zinc Binding Sites List in 3kyc
Zinc binding site 1 out of 1 in the Human Sumo E1 Complex with A SUMO1-Amp Mimic


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Sumo E1 Complex with A SUMO1-Amp Mimic within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn641

b:62.3
occ:1.00
SG B:CYS158 2.1 56.4 1.0
SG B:CYS161 2.1 62.4 1.0
SG B:CYS441 2.2 65.6 1.0
SG B:CYS444 2.5 63.2 1.0
CB B:CYS441 3.1 65.9 1.0
CB B:CYS444 3.2 63.7 1.0
CB B:CYS158 3.2 56.9 1.0
CB B:CYS161 3.4 64.2 1.0
N B:CYS161 3.4 62.4 1.0
CA B:CYS161 3.4 65.0 1.0
N B:CYS158 3.6 58.6 1.0
N B:CYS444 3.8 64.7 1.0
CA B:CYS158 3.9 56.9 1.0
C B:GLU160 4.1 60.0 1.0
CA B:CYS444 4.1 64.8 1.0
C B:CYS158 4.3 56.7 1.0
O B:CYS158 4.4 56.2 1.0
O B:GLU160 4.6 59.4 1.0
O B:HOH695 4.6 58.7 1.0
CA B:CYS441 4.6 66.9 1.0
N B:GLU160 4.7 56.2 1.0
CB B:VAL443 4.8 63.3 1.0
C B:GLU157 4.8 60.6 1.0
C B:CYS161 4.9 67.0 1.0
CA B:GLU160 4.9 57.6 1.0
C B:VAL443 4.9 64.1 1.0
O B:HOH776 5.0 61.1 1.0
O B:ASN438 5.0 75.0 1.0
C B:CYS444 5.0 65.6 1.0

Reference:

S.K.Olsen, A.D.Capili, X.Lu, D.S.Tan, C.D.Lima. Active Site Remodelling Accompanies Thioester Bond Formation in the Sumo E1. Nature V. 463 906 2010.
ISSN: ISSN 0028-0836
PubMed: 20164921
DOI: 10.1038/NATURE08765
Page generated: Wed Dec 16 04:31:22 2020

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