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

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

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 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 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 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 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

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