Atomistry » Zinc » PDB 1bj6-1bv3 » 1bkc
Atomistry »
  Zinc »
    PDB 1bj6-1bv3 »
      1bkc »

Zinc in PDB 1bkc: Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace)

Protein crystallography data

The structure of Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace), PDB code: 1bkc was solved by K.Maskos, C.Fernandez-Catalan, W.Bode, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 61.380, 126.270, 81.270, 90.00, 107.41, 90.00
R / Rfree (%) 18 / 27

Zinc Binding Sites:

The binding sites of Zinc atom in the Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace) (pdb code 1bkc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace), PDB code: 1bkc:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1bkc

Go back to Zinc Binding Sites List in 1bkc
Zinc binding site 1 out of 4 in the Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:25.6
occ:1.00
NE2 A:HIS415 2.3 10.1 1.0
NE2 A:HIS409 2.3 10.1 1.0
NE2 A:HIS405 2.4 8.8 1.0
O4 A:INN2 2.4 11.5 1.0
O A:INN2 2.4 15.9 1.0
N A:INN2 2.9 14.1 1.0
C A:INN2 3.0 14.5 1.0
CD2 A:HIS405 3.0 5.7 1.0
CD2 A:HIS409 3.2 10.6 1.0
CD2 A:HIS415 3.2 11.3 1.0
CE1 A:HIS415 3.2 9.7 1.0
CE1 A:HIS409 3.3 12.9 1.0
CE1 A:HIS405 3.4 10.4 1.0
O A:HOH601 4.0 14.1 1.0
CG A:HIS405 4.3 7.3 1.0
O A:HOH600 4.3 35.5 1.0
ND1 A:HIS415 4.3 10.4 1.0
CG A:HIS409 4.3 10.0 1.0
CG A:HIS415 4.3 11.2 1.0
ND1 A:HIS409 4.3 10.9 1.0
OE1 A:GLU406 4.4 11.9 1.0
C0 A:INN2 4.4 10.5 1.0
ND1 A:HIS405 4.4 7.5 1.0
CA A:INN2 4.4 10.3 1.0
CE A:MET435 4.5 11.6 1.0
O A:HOH605 4.5 14.4 1.0
CB A:INN2 4.5 10.8 1.0
OE2 A:GLU406 4.7 11.4 1.0
CD A:GLU406 4.9 12.4 1.0
O A:HOH778 5.0 43.3 1.0

Zinc binding site 2 out of 4 in 1bkc

Go back to Zinc Binding Sites List in 1bkc
Zinc binding site 2 out of 4 in the Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1

b:31.2
occ:1.00
NE2 C:HIS409 2.4 9.4 1.0
NE2 C:HIS405 2.4 11.4 1.0
NE2 C:HIS415 2.4 20.0 1.0
O4 C:INN2 2.5 19.7 1.0
O C:INN2 2.6 20.5 1.0
N C:INN2 2.9 19.5 1.0
C C:INN2 3.1 20.0 1.0
CD2 C:HIS405 3.1 9.7 1.0
CD2 C:HIS415 3.2 16.7 1.0
CD2 C:HIS409 3.2 9.9 1.0
CE1 C:HIS409 3.3 9.2 1.0
CE1 C:HIS405 3.4 13.0 1.0
CE1 C:HIS415 3.4 19.1 1.0
O C:HOH622 3.9 15.9 1.0
ND1 C:HIS409 4.3 8.1 1.0
CG C:HIS415 4.3 18.3 1.0
CG C:HIS405 4.3 11.4 1.0
CG C:HIS409 4.4 7.6 1.0
OE1 C:GLU406 4.4 15.1 1.0
ND1 C:HIS415 4.4 18.6 1.0
ND1 C:HIS405 4.4 10.8 1.0
C0 C:INN2 4.5 14.4 1.0
CA C:INN2 4.6 13.2 1.0
O C:HOH787 4.7 17.9 1.0
CB C:INN2 4.7 9.8 1.0
CE C:MET435 4.7 11.3 1.0
OE2 C:GLU406 4.8 16.2 1.0
O C:HOH792 4.8 41.3 1.0
CD C:GLU406 5.0 14.8 1.0

Zinc binding site 3 out of 4 in 1bkc

Go back to Zinc Binding Sites List in 1bkc
Zinc binding site 3 out of 4 in the Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace) within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn1

b:28.8
occ:1.00
NE2 E:HIS405 2.4 14.2 1.0
NE2 E:HIS415 2.4 18.5 1.0
NE2 E:HIS409 2.4 10.6 1.0
O E:INN2 2.4 20.4 1.0
O4 E:INN2 2.5 15.5 1.0
N E:INN2 3.0 17.1 1.0
C E:INN2 3.1 18.2 1.0
CD2 E:HIS415 3.2 15.8 1.0
CD2 E:HIS409 3.2 9.0 1.0
CD2 E:HIS405 3.2 15.1 1.0
CE1 E:HIS405 3.3 16.8 1.0
CE1 E:HIS415 3.3 16.6 1.0
CE1 E:HIS409 3.4 8.0 1.0
O E:HOH643 3.9 13.6 1.0
CG E:HIS415 4.3 17.2 1.0
CG E:HIS409 4.3 7.7 1.0
ND1 E:HIS405 4.3 13.3 1.0
ND1 E:HIS415 4.4 16.5 1.0
CG E:HIS405 4.4 14.3 1.0
OE1 E:GLU406 4.4 12.3 1.0
ND1 E:HIS409 4.4 8.7 1.0
C0 E:INN2 4.5 14.6 1.0
CA E:INN2 4.6 13.5 1.0
CE E:MET435 4.6 14.7 1.0
O E:HOH690 4.6 13.6 1.0
CB E:INN2 4.6 12.4 1.0
OE2 E:GLU406 4.7 12.7 1.0
O E:HOH691 4.8 36.2 1.0
CD E:GLU406 4.9 12.9 1.0

Zinc binding site 4 out of 4 in 1bkc

Go back to Zinc Binding Sites List in 1bkc
Zinc binding site 4 out of 4 in the Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Catalytic Domain of Tnf-Alpha Converting Enzyme (Tace) within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Zn1

b:24.4
occ:1.00
NE2 I:HIS405 2.3 5.6 1.0
O I:INN2 2.3 13.4 1.0
NE2 I:HIS409 2.4 13.9 1.0
NE2 I:HIS415 2.4 7.0 1.0
O4 I:INN2 2.5 8.4 1.0
N I:INN2 2.9 11.9 1.0
CD2 I:HIS405 3.0 3.6 1.0
CD2 I:HIS415 3.0 7.4 1.0
C I:INN2 3.0 13.3 1.0
CD2 I:HIS409 3.2 13.0 1.0
CE1 I:HIS405 3.3 9.3 1.0
CE1 I:HIS409 3.4 12.7 1.0
CE1 I:HIS415 3.5 9.8 1.0
CG I:HIS405 4.2 6.1 1.0
CG I:HIS415 4.3 9.5 1.0
CG I:HIS409 4.3 10.9 1.0
ND1 I:HIS405 4.4 6.7 1.0
C0 I:INN2 4.4 8.3 1.0
OE1 I:GLU406 4.4 10.4 1.0
ND1 I:HIS409 4.4 11.2 1.0
ND1 I:HIS415 4.4 9.3 1.0
CA I:INN2 4.4 9.6 1.0
CB I:INN2 4.5 8.4 1.0
OE2 I:GLU406 4.7 9.6 1.0
CE I:MET435 4.7 9.0 1.0
CD I:GLU406 4.9 12.4 1.0

Reference:

K.Maskos, C.Fernandez-Catalan, R.Huber, G.P.Bourenkov, H.Bartunik, G.A.Ellestad, P.Reddy, M.F.Wolfson, C.T.Rauch, B.J.Castner, R.Davis, H.R.Clarke, M.Petersen, J.N.Fitzner, D.P.Cerretti, C.J.March, R.J.Paxton, R.A.Black, W.Bode. Crystal Structure of the Catalytic Domain of Human Tumor Necrosis Factor-Alpha-Converting Enzyme. Proc.Natl.Acad.Sci.Usa V. 95 3408 1998.
ISSN: ISSN 0027-8424
PubMed: 9520379
DOI: 10.1073/PNAS.95.7.3408
Page generated: Wed Dec 16 02:45:53 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy