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Calcium in PDB 3hbt: The Structure of Native G-Actin

Protein crystallography data

The structure of The Structure of Native G-Actin, PDB code: 3hbt was solved by H.Wang, R.C.Robinson, L.D.Burtnick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.64 / 2.70
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 95.731, 95.731, 96.948, 90.00, 90.00, 120.00
R / Rfree (%) 20.2 / 25.7

Calcium Binding Sites:

The binding sites of Calcium atom in the The Structure of Native G-Actin (pdb code 3hbt). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the The Structure of Native G-Actin, PDB code: 3hbt:

Calcium binding site 1 out of 1 in 3hbt

Go back to Calcium Binding Sites List in 3hbt
Calcium binding site 1 out of 1 in the The Structure of Native G-Actin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Structure of Native G-Actin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1401

b:40.8
occ:1.00
O A:HOH377 2.2 24.1 1.0
O2B A:ATP1380 2.3 39.2 1.0
O A:HOH389 2.3 37.2 1.0
O A:HOH388 2.3 27.5 1.0
O A:HOH380 2.4 28.2 1.0
O A:HOH384 2.4 34.4 1.0
O3G A:ATP1380 2.4 36.2 1.0
PG A:ATP1380 3.4 37.6 1.0
PB A:ATP1380 3.5 38.1 1.0
O1G A:ATP1380 3.7 35.1 1.0
O3B A:ATP1380 3.9 40.0 1.0
O3A A:ATP1380 4.1 38.4 1.0
CA A:GLY13 4.2 46.6 1.0
O A:HOH386 4.3 22.5 1.0
NZ A:LYS18 4.3 41.9 1.0
O1A A:ATP1380 4.3 41.3 1.0
OD2 A:ASP154 4.3 50.1 1.0
OE1 A:GLN137 4.4 43.5 1.0
PA A:ATP1380 4.6 40.5 1.0
O A:ASN12 4.6 48.9 1.0
CD A:GLN137 4.7 42.2 1.0
O A:HOH385 4.7 25.6 1.0
O A:HOH382 4.7 29.8 1.0
O2G A:ATP1380 4.8 38.8 1.0
O1B A:ATP1380 4.8 39.5 1.0
OD1 A:ASP154 4.8 52.2 1.0
O2A A:ATP1380 4.8 39.6 1.0
OD1 A:ASP11 4.9 49.5 1.0
OD2 A:ASP11 4.9 52.7 1.0
NE2 A:GLN137 4.9 41.5 1.0

Reference:

H.Wang, R.C.Robinson, L.D.Burtnick. The Structure of Native G-Actin Cytoskeleton (Hoboken) V. 67 456 2010.
ISSN: ISSN 1949-3584
PubMed: 20540085
DOI: 10.1002/CM.20458
Page generated: Sat Dec 12 04:13:51 2020

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