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Arsenic in PDB 9o9i: Crystal Structure of Mouse VPS29 Bound to DENND4C Peptide (Re- Refinement)

Protein crystallography data

The structure of Crystal Structure of Mouse VPS29 Bound to DENND4C Peptide (Re- Refinement), PDB code: 9o9i was solved by K.-E.Chen, B.Collins, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.32 / 2.35
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 42.899, 42.899, 172.743, 90, 90, 120
R / Rfree (%) 18.9 / 25.3

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of Mouse VPS29 Bound to DENND4C Peptide (Re- Refinement) (pdb code 9o9i). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of Mouse VPS29 Bound to DENND4C Peptide (Re- Refinement), PDB code: 9o9i:

Arsenic binding site 1 out of 1 in 9o9i

Go back to Arsenic Binding Sites List in 9o9i
Arsenic binding site 1 out of 1 in the Crystal Structure of Mouse VPS29 Bound to DENND4C Peptide (Re- Refinement)


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Mouse VPS29 Bound to DENND4C Peptide (Re- Refinement) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As201

b:164.1
occ:1.00
AS A:CAC201 0.0 164.1 1.0
O1 A:CAC201 1.7 89.6 1.0
O2 A:CAC201 1.7 89.1 1.0
C1 A:CAC201 2.0 81.6 1.0
C2 A:CAC201 2.0 93.2 1.0
NE2 A:HIS92 3.1 58.6 1.0
CE1 A:HIS92 3.8 52.2 1.0
OE2 A:GLU75 4.0 69.4 1.0
OE1 A:GLU75 4.0 77.1 1.0
CD2 A:HIS92 4.2 56.1 1.0
NH1 A:ARG64 4.3 54.1 1.0
CD A:GLU75 4.4 74.6 1.0
CD A:ARG64 4.6 51.5 1.0
CA A:ASP66 4.9 51.9 1.0
O A:GLY65 5.0 40.5 1.0

Reference:

C.Anton-Plagaro, K.E.Chen, Q.Guo, M.Liu, A.J.Evans, P.A.Lewis, K.J.Heesom, K.A.Wilkinson, B.M.Collins, P.J.Cullen. Mapping of Endosomal Proximity Proteomes Reveals Retromer As A Hub For Rab Gtpase Regulation. Nat Commun V. 16 6990 2025.
ISSN: ESSN 2041-1723
PubMed: 40738907
DOI: 10.1038/S41467-025-61802-1
Page generated: Fri Aug 22 21:11:03 2025

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