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Chlorine in PDB 2esp: Human Ubiquitin-Conjugating Enzyme (E2) UBCH5B Mutant ILE88ALA

Enzymatic activity of Human Ubiquitin-Conjugating Enzyme (E2) UBCH5B Mutant ILE88ALA

All present enzymatic activity of Human Ubiquitin-Conjugating Enzyme (E2) UBCH5B Mutant ILE88ALA:
6.3.2.19;

Protein crystallography data

The structure of Human Ubiquitin-Conjugating Enzyme (E2) UBCH5B Mutant ILE88ALA, PDB code: 2esp was solved by E.Ozkan, H.Yu, J.Deisenhofer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.58 / 1.52
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.877, 49.224, 62.128, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 23.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human Ubiquitin-Conjugating Enzyme (E2) UBCH5B Mutant ILE88ALA (pdb code 2esp). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Human Ubiquitin-Conjugating Enzyme (E2) UBCH5B Mutant ILE88ALA, PDB code: 2esp:

Chlorine binding site 1 out of 1 in 2esp

Go back to Chlorine Binding Sites List in 2esp
Chlorine binding site 1 out of 1 in the Human Ubiquitin-Conjugating Enzyme (E2) UBCH5B Mutant ILE88ALA


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Ubiquitin-Conjugating Enzyme (E2) UBCH5B Mutant ILE88ALA within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl148

b:19.6
occ:1.00
NZ A:LYS8 3.1 19.3 1.0
O A:HOH163 3.1 17.8 1.0
CE A:MET1 3.4 24.0 1.0
CD A:ARG5 3.8 16.4 1.0
CE A:LYS4 3.8 27.1 1.0
CE A:LYS8 3.8 21.3 1.0
CB A:ARG5 4.0 16.6 1.0
CA A:ARG5 4.0 15.9 1.0
CD A:LYS8 4.1 20.0 1.0
N A:ARG5 4.4 15.5 1.0
CG A:ARG5 4.4 16.4 1.0
CD A:LYS4 4.5 22.9 1.0
NZ A:LYS4 4.5 23.8 1.0
CG A:LYS4 4.6 19.6 1.0
C A:LYS4 4.9 15.4 1.0
O A:HOH243 4.9 27.7 1.0

Reference:

E.Ozkan, H.Yu, J.Deisenhofer. Mechanistic Insight Into the Allosteric Activation of A Ubiquitin-Conjugating Enzyme By Ring-Type Ubiquitin Ligases Proc.Natl.Acad.Sci.Usa V. 102 18890 2005.
ISSN: ISSN 0027-8424
PubMed: 16365295
DOI: 10.1073/PNAS.0509418102
Page generated: Sat Jul 20 06:50:06 2024

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