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Calcium in PDB 1uzj: Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form.

Protein crystallography data

The structure of Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form., PDB code: 1uzj 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) 30.0 / 2.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 43.100, 105.600, 65.000, 90.00, 104.20, 90.00
R / Rfree (%) 24.7 / 31.8

Calcium Binding Sites:

The binding sites of Calcium atom in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form. (pdb code 1uzj). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 6 binding sites of Calcium where determined in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form., PDB code: 1uzj:
Jump to Calcium binding site number: 1; 2; 3; 4; 5; 6;

Calcium binding site 1 out of 6 in 1uzj

Go back to Calcium Binding Sites List in 1uzj
Calcium binding site 1 out of 6 in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form.


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, Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1648

b:28.2
occ:1.00
OD1 A:ASN1504 2.2 18.1 1.0
O A:VAL1488 2.5 20.9 1.0
O A:SER1508 2.5 18.9 1.0
OD2 A:ASP1487 2.5 33.2 1.0
OE1 A:GLU1490 2.6 21.2 1.0
O A:THR1505 2.6 29.7 1.0
OD1 A:ASP1487 3.1 20.2 1.0
CG A:ASP1487 3.2 35.8 1.0
CG A:ASN1504 3.4 24.4 1.0
CD A:GLU1490 3.4 24.6 1.0
C A:SER1508 3.5 20.2 1.0
OE2 A:GLU1490 3.5 19.3 1.0
C A:VAL1488 3.7 24.9 1.0
N A:SER1508 3.7 27.1 1.0
CA A:SER1508 3.8 25.0 1.0
C A:THR1505 3.9 29.0 1.0
C A:GLY1507 3.9 31.1 1.0
ND2 A:ASN1504 4.0 21.0 1.0
N A:GLY1507 4.0 27.1 1.0
N A:THR1505 4.1 17.9 1.0
O A:GLY1507 4.1 34.4 1.0
O A:HOH2008 4.2 46.4 1.0
N A:GLU1490 4.4 6.6 1.0
N A:VAL1488 4.4 29.3 1.0
CA A:ASN1489 4.4 19.3 1.0
N A:ASN1489 4.5 22.8 1.0
CA A:GLY1507 4.6 29.1 1.0
CB A:ASN1504 4.6 17.6 1.0
CA A:VAL1488 4.7 29.2 1.0
N A:TYR1509 4.7 21.6 1.0
CA A:THR1505 4.7 21.4 1.0
CB A:ASP1487 4.7 36.5 1.0
C A:PRO1506 4.7 26.6 1.0
N A:PRO1506 4.8 25.9 1.0
C A:ASN1504 4.8 18.1 1.0
CG A:GLU1490 4.8 20.6 1.0
CA A:PRO1506 4.8 23.3 1.0
CA A:ASN1504 4.9 18.7 1.0
C A:ASN1489 5.0 16.4 1.0
C A:ASP1487 5.0 33.9 1.0

Calcium binding site 2 out of 6 in 1uzj

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Calcium binding site 2 out of 6 in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1649

b:24.4
occ:1.00
O A:ILE1607 2.3 21.2 1.0
O A:SER1628 2.3 24.3 1.0
OD1 A:ASN1624 2.3 32.5 1.0
O A:HOH2068 2.4 19.0 1.0
OE2 A:GLU1609 2.4 23.7 1.0
OD1 A:ASP1606 2.5 21.2 1.0
O A:THR1625 2.6 14.3 1.0
OD2 A:ASP1606 2.9 33.8 1.0
CG A:ASP1606 3.1 30.1 1.0
CD A:GLU1609 3.3 25.0 1.0
CG A:ASN1624 3.3 30.4 1.0
C A:SER1628 3.4 30.1 1.0
C A:ILE1607 3.4 17.5 1.0
OE1 A:GLU1609 3.4 29.2 1.0
N A:SER1628 3.5 31.5 1.0
ND2 A:ASN1624 3.7 30.6 1.0
C A:THR1625 3.8 22.3 1.0
CA A:SER1628 3.9 30.4 1.0
CA A:ASP1608 4.0 24.1 1.0
N A:GLY1627 4.0 25.4 1.0
N A:THR1625 4.1 23.6 1.0
N A:GLU1609 4.1 17.9 1.0
N A:ASP1608 4.1 18.0 1.0
N A:ILE1607 4.2 15.5 1.0
C A:GLY1627 4.3 30.0 1.0
CA A:ILE1607 4.5 19.9 1.0
N A:PHE1629 4.5 28.0 1.0
CB A:ASP1606 4.6 24.3 1.0
CA A:THR1625 4.6 26.3 1.0
C A:ASP1608 4.6 22.5 1.0
CA A:GLY1627 4.6 20.8 1.0
CG A:GLU1609 4.7 24.7 1.0
CB A:ASN1624 4.7 30.5 1.0
CB A:PHE1629 4.7 25.7 1.0
N A:PHE1626 4.8 23.3 1.0
O A:GLY1594 4.8 24.7 1.0
CB A:ILE1607 4.9 24.2 1.0
C A:PHE1626 4.9 22.0 1.0
C A:ASP1606 4.9 16.4 1.0
OG1 A:THR1625 4.9 20.4 1.0
CA A:PHE1626 4.9 19.7 1.0
CA A:ASN1624 5.0 25.6 1.0
CA A:PHE1629 5.0 24.6 1.0
C A:ASN1624 5.0 26.9 1.0

Calcium binding site 3 out of 6 in 1uzj

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Calcium binding site 3 out of 6 in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca2648

b:27.7
occ:1.00
O B:VAL2488 2.2 21.6 1.0
OE1 B:GLU2490 2.5 29.7 1.0
O B:SER2508 2.5 29.0 1.0
O B:THR2505 2.5 21.2 1.0
OD1 B:ASP2487 2.6 39.5 1.0
OD1 B:ASN2504 2.6 21.4 1.0
OD2 B:ASP2487 2.8 44.6 1.0
CG B:ASP2487 3.1 44.1 1.0
O B:GLY2507 3.2 38.9 1.0
CD B:GLU2490 3.4 29.6 1.0
C B:VAL2488 3.5 25.0 1.0
OE2 B:GLU2490 3.5 36.4 1.0
CG B:ASN2504 3.6 19.1 1.0
C B:SER2508 3.6 30.5 1.0
C B:GLY2507 3.7 35.6 1.0
C B:THR2505 3.8 26.1 1.0
N B:THR2505 4.0 19.4 1.0
ND2 B:ASN2504 4.0 21.8 1.0
N B:GLY2507 4.1 27.3 1.0
CA B:SER2508 4.1 32.6 1.0
N B:SER2508 4.1 31.5 1.0
N B:VAL2488 4.1 34.6 1.0
CA B:VAL2488 4.4 28.8 1.0
N B:ASN2489 4.4 22.4 1.0
CA B:ASN2489 4.4 19.9 1.0
N B:GLU2490 4.5 15.3 1.0
CA B:GLY2507 4.6 31.0 1.0
CB B:ASP2487 4.6 46.8 1.0
CA B:THR2505 4.6 21.5 1.0
C B:PRO2506 4.7 31.5 1.0
N B:PRO2506 4.7 25.2 1.0
N B:TYR2509 4.8 26.6 1.0
CA B:PRO2506 4.8 27.8 1.0
CG B:GLU2490 4.8 28.0 1.0
CB B:ASN2504 4.8 18.3 1.0
CB B:VAL2488 4.9 28.5 1.0
OG1 B:THR2505 4.9 16.6 1.0
C B:ASN2504 4.9 20.3 1.0
CA B:ASN2504 4.9 19.4 1.0
C B:ASP2487 4.9 41.0 1.0
CB B:TYR2509 5.0 23.2 1.0

Calcium binding site 4 out of 6 in 1uzj

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Calcium binding site 4 out of 6 in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca2649

b:27.2
occ:1.00
O B:SER2628 2.3 26.0 1.0
OD1 B:ASN2624 2.3 31.2 1.0
O B:ILE2607 2.4 23.0 1.0
OE2 B:GLU2609 2.4 21.1 1.0
O B:THR2625 2.5 26.9 1.0
O B:HOH2067 2.5 8.9 1.0
OD1 B:ASP2606 2.7 12.2 1.0
OD2 B:ASP2606 2.8 19.1 1.0
CG B:ASP2606 3.1 24.8 1.0
C B:SER2628 3.3 30.0 1.0
CD B:GLU2609 3.3 20.6 1.0
CG B:ASN2624 3.5 32.3 1.0
N B:SER2628 3.5 31.5 1.0
OE1 B:GLU2609 3.5 29.2 1.0
C B:ILE2607 3.6 22.3 1.0
C B:THR2625 3.7 26.8 1.0
CA B:SER2628 3.7 27.9 1.0
N B:GLY2627 3.9 26.4 1.0
N B:THR2625 4.1 29.1 1.0
ND2 B:ASN2624 4.1 23.0 1.0
C B:GLY2627 4.1 31.6 1.0
N B:ILE2607 4.3 18.4 1.0
N B:GLU2609 4.3 22.4 1.0
CA B:ASP2608 4.4 25.2 1.0
N B:ASP2608 4.5 21.2 1.0
N B:PHE2629 4.5 30.8 1.0
CA B:THR2625 4.5 27.8 1.0
CA B:ILE2607 4.5 23.1 1.0
CA B:GLY2627 4.5 26.1 1.0
CB B:ASP2606 4.6 22.7 1.0
CB B:ASN2624 4.7 31.5 1.0
N B:PHE2626 4.7 29.9 1.0
CB B:PHE2629 4.7 30.8 1.0
CG B:GLU2609 4.7 26.1 1.0
O B:GLY2627 4.7 35.9 1.0
C B:PHE2626 4.8 26.6 1.0
CA B:PHE2626 4.8 29.0 1.0
C B:ASN2624 4.9 30.7 1.0
O B:GLY2594 4.9 21.9 1.0
OG1 B:THR2625 5.0 34.5 1.0
C B:ASP2608 5.0 21.1 1.0
CB B:ILE2607 5.0 25.1 1.0
C B:ASP2606 5.0 21.1 1.0
CA B:PHE2629 5.0 30.8 1.0
CA B:ASN2624 5.0 30.4 1.0

Calcium binding site 5 out of 6 in 1uzj

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Calcium binding site 5 out of 6 in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 5 of Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca3648

b:29.6
occ:1.00
OD1 C:ASN3504 2.3 14.9 1.0
O C:VAL3488 2.4 22.7 1.0
O C:THR3505 2.5 34.1 1.0
O C:SER3508 2.6 34.4 1.0
OE1 C:GLU3490 2.9 30.0 1.0
OD2 C:ASP3487 3.0 35.4 1.0
OD1 C:ASP3487 3.1 26.1 1.0
CG C:ASN3504 3.3 27.6 1.0
CG C:ASP3487 3.4 34.6 1.0
C C:SER3508 3.5 36.2 1.0
N C:SER3508 3.5 32.6 1.0
OE2 C:GLU3490 3.5 27.9 1.0
CD C:GLU3490 3.5 29.5 1.0
C C:VAL3488 3.5 26.1 1.0
C C:THR3505 3.7 37.7 1.0
CA C:SER3508 3.8 36.5 1.0
ND2 C:ASN3504 3.8 24.5 1.0
N C:GLY3507 4.0 36.2 1.0
N C:THR3505 4.1 28.0 1.0
C C:GLY3507 4.1 38.3 1.0
CA C:ASN3489 4.3 23.0 1.0
N C:ASN3489 4.4 23.7 1.0
N C:VAL3488 4.4 32.4 1.0
O C:HOH2010 4.4 24.3 1.0
CA C:VAL3488 4.5 30.3 1.0
CA C:THR3505 4.6 32.3 1.0
CA C:GLY3507 4.6 36.8 1.0
N C:GLU3490 4.7 21.7 1.0
CB C:ASN3504 4.7 24.9 1.0
C C:PRO3506 4.7 38.4 1.0
N C:PRO3506 4.7 40.9 1.0
N C:TYR3509 4.7 33.2 1.0
CA C:PRO3506 4.8 38.2 1.0
O C:GLY3507 4.9 43.5 1.0
CG C:GLU3490 4.9 29.3 1.0
OG1 C:THR3505 4.9 28.1 1.0
CA C:ASN3504 5.0 28.3 1.0
C C:ASN3504 5.0 30.5 1.0
CB C:ASP3487 5.0 32.0 1.0

Calcium binding site 6 out of 6 in 1uzj

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Calcium binding site 6 out of 6 in the Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 6 of Integrin Binding CBEGF22-TB4-CBEGF33 Fragment of Human Fibrillin-1, Holo Form. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Ca3649

b:42.3
occ:1.00
O C:SER3628 2.1 28.7 1.0
O C:THR3625 2.4 57.7 1.0
OD1 C:ASP3606 2.5 44.4 1.0
OE2 C:GLU3609 2.6 25.8 1.0
O C:ILE3607 2.6 38.8 1.0
OD1 C:ASN3624 2.7 43.8 1.0
OD2 C:ASP3606 3.0 34.6 1.0
CG C:ASP3606 3.1 45.7 1.0
C C:SER3628 3.1 36.4 1.0
N C:SER3628 3.1 45.7 1.0
CD C:GLU3609 3.4 34.9 1.0
CA C:SER3628 3.5 41.0 1.0
OE1 C:GLU3609 3.5 29.3 1.0
C C:THR3625 3.6 55.2 1.0
C C:ILE3607 3.7 44.5 1.0
N C:GLY3627 3.7 48.4 1.0
CG C:ASN3624 3.8 51.1 1.0
C C:GLY3627 3.9 46.5 1.0
N C:THR3625 4.0 50.2 1.0
CA C:GLY3627 4.3 45.7 1.0
N C:ILE3607 4.3 46.5 1.0
N C:PHE3629 4.3 33.2 1.0
ND2 C:ASN3624 4.4 50.5 1.0
CA C:THR3625 4.4 52.2 1.0
N C:GLU3609 4.4 41.1 1.0
CA C:ASP3608 4.5 46.4 1.0
N C:ASP3608 4.5 42.4 1.0
O C:GLY3594 4.5 42.7 1.0
CB C:ASP3606 4.5 43.6 1.0
N C:PHE3626 4.5 56.4 1.0
C C:PHE3626 4.6 53.3 1.0
CA C:ILE3607 4.6 43.3 1.0
O C:GLY3627 4.7 45.7 1.0
CA C:PHE3626 4.7 53.3 1.0
OG1 C:THR3625 4.7 42.8 1.0
CB C:PHE3629 4.8 32.4 1.0
C C:ASP3606 4.8 46.3 1.0
CG C:GLU3609 4.8 36.9 1.0
CA C:PHE3629 4.9 34.4 1.0
CB C:SER3628 4.9 41.1 1.0

Reference:

S.S.J.Lee, V.Knott, J.Jovanovi, K.Harlos, J.Grimes, L.Choulier, H.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: Thu Jul 11 23:45:43 2024

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