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Calcium in PDB 1uzk: Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Ca Bound to CBEGF23 Domain Only

Protein crystallography data

The structure of Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Ca Bound to CBEGF23 Domain Only, PDB code: 1uzk was solved by S.S.J.Lee, V.Knott, K.Harlos, P.A.Handford, D.I.Stuart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.35
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 42.500, 70.800, 102.600, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 26.1

Calcium Binding Sites:

The binding sites of Calcium atom in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Ca Bound to CBEGF23 Domain Only (pdb code 1uzk). 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 Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Ca Bound to CBEGF23 Domain Only, PDB code: 1uzk:

Calcium binding site 1 out of 1 in 1uzk

Go back to Calcium Binding Sites List in 1uzk
Calcium binding site 1 out of 1 in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Ca Bound to CBEGF23 Domain Only


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Ca Bound to CBEGF23 Domain Only within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2512

b:19.4
occ:1.00
O A:ILE1607 2.4 18.0 1.0
OD1 A:ASN1624 2.4 19.3 1.0
O A:HOH2114 2.4 19.2 1.0
O A:SER1628 2.5 17.7 1.0
OE2 A:GLU1609 2.5 19.4 1.0
OD1 A:ASP1606 2.5 19.4 1.0
O A:THR1625 2.5 22.1 1.0
OD2 A:ASP1606 2.7 24.5 1.0
CG A:ASP1606 3.0 21.0 1.0
CG A:ASN1624 3.4 19.8 1.0
CD A:GLU1609 3.5 19.9 1.0
C A:SER1628 3.5 20.8 1.0
C A:ILE1607 3.6 17.1 1.0
N A:SER1628 3.6 20.6 1.0
C A:THR1625 3.7 23.4 1.0
ND2 A:ASN1624 3.8 22.0 1.0
OE1 A:GLU1609 3.9 21.7 1.0
N A:THR1625 4.0 22.1 1.0
N A:GLY1627 4.0 23.0 1.0
CA A:SER1628 4.1 22.1 1.0
C A:GLY1627 4.2 20.7 1.0
N A:GLU1609 4.3 18.9 1.0
CA A:ASP1608 4.3 18.3 1.0
N A:ILE1607 4.4 17.4 1.0
N A:ASP1608 4.4 17.6 1.0
CA A:THR1625 4.5 22.5 1.0
CB A:ASP1606 4.5 19.9 1.0
CA A:ILE1607 4.5 17.0 1.0
CA A:GLY1627 4.6 22.5 1.0
O A:GLY1594 4.6 16.9 1.0
N A:PHE1629 4.6 21.3 1.0
N A:PHE1626 4.7 24.7 1.0
CB A:ASN1624 4.7 21.3 1.0
CG A:GLU1609 4.8 20.3 1.0
C A:ASN1624 4.8 23.4 1.0
CB A:PHE1629 4.8 20.0 1.0
C A:PHE1626 4.9 24.5 1.0
CA A:PHE1626 4.9 23.8 1.0
OG1 A:THR1625 4.9 28.7 1.0
CA A:ASN1624 4.9 21.1 1.0
C A:ASP1608 4.9 18.3 1.0
C A:ASP1606 4.9 17.9 1.0

Reference:

S.S.J.Lee, V.Knott, J.Jovanovi, K.Harlos, J.M.Grimes, L.Choulier, H.J.Mardon, D.I.Stuart, P.A.Handford. Structure of the Integrin Binding Fragment From Fibrillin-1 Gives New Insights Into Microfibril Organization Structure V. 12 717 2004.
ISSN: ISSN 0969-2126
PubMed: 15062093
DOI: 10.1016/J.STR.2004.02.023
Page generated: Sat Dec 12 03:23:55 2020

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