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Lead in PDB 5vfg: Synaptotagmin 1 C2B Domain, Lead-Bound (High Occupancy)

Protein crystallography data

The structure of Synaptotagmin 1 C2B Domain, Lead-Bound (High Occupancy), PDB code: 5vfg was solved by A.B.Taylor, P.J.Hart, T.I.Igumenova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.64 / 1.82
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.524, 41.277, 83.474, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 25.9

Lead Binding Sites:

The binding sites of Lead atom in the Synaptotagmin 1 C2B Domain, Lead-Bound (High Occupancy) (pdb code 5vfg). This binding sites where shown within 5.0 Angstroms radius around Lead atom.
In total only one binding site of Lead was determined in the Synaptotagmin 1 C2B Domain, Lead-Bound (High Occupancy), PDB code: 5vfg:

Lead binding site 1 out of 1 in 5vfg

Go back to Lead Binding Sites List in 5vfg
Lead binding site 1 out of 1 in the Synaptotagmin 1 C2B Domain, Lead-Bound (High Occupancy)


Mono view


Stereo pair view

A full contact list of Lead with other atoms in the Pb binding site number 1 of Synaptotagmin 1 C2B Domain, Lead-Bound (High Occupancy) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pb501

b:19.2
occ:1.00
OD1 A:ASP365 2.4 29.6 1.0
OD2 A:ASP363 2.5 16.8 1.0
OD1 A:ASP303 2.6 23.7 1.0
OD1 A:ASP363 2.6 13.2 1.0
O A:TYR364 2.6 20.8 1.0
OD2 A:ASP309 2.7 15.8 1.0
OD2 A:ASP303 2.8 20.1 1.0
O A:HOH607 2.8 21.0 1.0
CG A:ASP363 2.9 15.8 1.0
CG A:ASP303 3.0 18.6 1.0
CG A:ASP365 3.4 29.1 1.0
CG A:ASP309 3.6 14.4 1.0
C A:TYR364 3.7 18.4 1.0
OD2 A:ASP365 4.0 30.6 1.0
CB A:ASP309 4.0 15.2 1.0
CA A:ASP365 4.2 21.5 1.0
N A:ASP365 4.3 23.3 1.0
CB A:ASP363 4.4 16.8 1.0
O A:HOH670 4.4 25.8 1.0
CB A:ASP365 4.4 27.5 1.0
N A:ASP309 4.4 13.8 1.0
CB A:ASP303 4.5 19.6 1.0
OD1 A:ASP309 4.5 16.4 1.0
N A:TYR364 4.6 19.1 1.0
CA A:TYR364 4.7 21.2 1.0
C A:ASP363 4.8 19.1 1.0
CA A:ASP309 4.9 16.7 1.0

Reference:

S.Katti, B.Her, A.K.Srivastava, A.B.Taylor, S.W.Lockless, T.I.Igumenova. High Affinity Interactions of PB2+with Synaptotagmin I. Metallomics V. 10 1211 2018.
ISSN: ESSN 1756-591X
PubMed: 30063057
DOI: 10.1039/C8MT00135A
Page generated: Mon Aug 18 22:58:08 2025

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