Zinc in PDB 3ayk: Catalytic Fragment of Human Fibroblast Collagenase Complexed with Cgs- 27023A, uc(Nmr), Minimized Average Structure

All present enzymatic activity of Catalytic Fragment of Human Fibroblast Collagenase Complexed with Cgs- 27023A, uc(Nmr), Minimized Average Structure:
3.4.24.7;

The structure of Catalytic Fragment of Human Fibroblast Collagenase Complexed with Cgs- 27023A, uc(Nmr), Minimized Average Structure also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Zinc atom in the Catalytic Fragment of Human Fibroblast Collagenase Complexed with Cgs- 27023A, uc(Nmr), Minimized Average Structure (pdb code 3ayk). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Catalytic Fragment of Human Fibroblast Collagenase Complexed with Cgs- 27023A, uc(Nmr), Minimized Average Structure, PDB code: 3ayk:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Catalytic Fragment of Human Fibroblast Collagenase Complexed with Cgs- 27023A, uc(Nmr), Minimized Average Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Catalytic Fragment of Human Fibroblast Collagenase Complexed with Cgs- 27023A, uc(Nmr), Minimized Average Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn170 b:0.4 occ:1.00 H50 A:CGS173 1.9 1.1 1.0 NE2 A:HIS128 2.0 0.4 1.0 NE2 A:HIS122 2.1 0.4 1.0 O48 A:CGS173 2.1 0.5 1.0 NE2 A:HIS118 2.1 0.5 1.0 O47 A:CGS173 2.3 0.5 1.0 N35 A:CGS173 2.7 0.4 1.0 C34 A:CGS173 2.8 0.4 1.0 CE1 A:HIS128 2.9 1.0 1.0 CE1 A:HIS118 2.9 0.7 1.0 CE1 A:HIS122 3.0 0.6 1.0 CD2 A:HIS128 3.0 0.6 1.0 HE1 A:HIS122 3.1 0.8 1.0 CD2 A:HIS118 3.1 0.6 1.0 HE1 A:HIS128 3.1 1.4 1.0 HE1 A:HIS118 3.2 0.9 1.0 CD2 A:HIS122 3.2 0.3 1.0 HD2 A:HIS128 3.3 1.2 1.0 HD2 A:HIS118 3.4 0.9 1.0 HD2 A:HIS122 3.5 0.5 1.0 H49 A:CGS173 3.6 0.4 1.0 HB A:CGS173 4.0 0.5 1.0 ND1 A:HIS118 4.0 0.7 1.0 ND1 A:HIS128 4.1 1.0 1.0 HE3 A:MET136 4.1 1.1 1.0 CG A:HIS118 4.1 0.4 1.0 CG A:HIS128 4.2 0.4 1.0 ND1 A:HIS122 4.2 0.6 1.0 CA A:CGS173 4.2 0.4 1.0 CG A:HIS122 4.3 0.3 1.0 HC1 A:CGS173 4.6 0.4 1.0 CB A:CGS173 4.6 0.4 1.0 HG21 A:CGS173 4.6 1.2 1.0 HA A:CGS173 4.7 0.3 1.0 HD1 A:HIS118 4.9 1.1 1.0 HA A:PRO138 4.9 0.7 1.0 O A:TYR137 4.9 0.5 1.0 HD1 A:HIS128 5.0 1.6 1.0

Zinc binding site 2 out of 2 in the Catalytic Fragment of Human Fibroblast Collagenase Complexed with Cgs- 27023A, uc(Nmr), Minimized Average Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Catalytic Fragment of Human Fibroblast Collagenase Complexed with Cgs- 27023A, uc(Nmr), Minimized Average Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn171 b:0.4 occ:1.00 ND1 A:HIS96 2.0 0.4 1.0 NE2 A:HIS68 2.0 0.5 1.0 NE2 A:HIS83 2.2 0.3 1.0 HG21 A:VAL64 2.6 1.0 1.0 HB3 A:HIS96 2.7 0.6 1.0 HE1 A:HIS83 2.7 0.5 1.0 CE1 A:HIS83 2.8 0.4 1.0 HB2 A:HIS96 2.9 0.5 1.0 CD2 A:HIS68 2.9 0.5 1.0 CG A:HIS96 2.9 0.3 1.0 CB A:HIS96 3.0 0.4 1.0 CE1 A:HIS68 3.0 0.5 1.0 HD2 A:HIS68 3.1 0.5 1.0 CE1 A:HIS96 3.1 0.4 1.0 OD2 A:ASP70 3.1 2.1 1.0 HE2 A:PHE74 3.2 0.4 1.0 HE1 A:HIS68 3.4 0.5 1.0 HE1 A:HIS96 3.4 0.5 1.0 CD2 A:HIS83 3.5 0.4 1.0 CG2 A:VAL64 3.6 0.3 1.0 HG12 A:VAL64 3.6 1.1 1.0 HG22 A:VAL64 3.9 1.1 1.0 HD2 A:HIS83 4.0 0.5 1.0 CG A:HIS68 4.0 0.5 1.0 HZ A:PHE74 4.0 0.4 1.0 ND1 A:HIS68 4.0 0.4 1.0 CE2 A:PHE74 4.1 0.4 1.0 HG23 A:VAL64 4.1 1.1 1.0 ND1 A:HIS83 4.1 0.4 1.0 CD2 A:HIS96 4.1 0.4 1.0 NE2 A:HIS96 4.2 0.3 1.0 CG A:ASP70 4.2 1.5 1.0 HB2 A:ASP70 4.4 1.0 1.0 CG A:HIS83 4.4 0.3 1.0 CZ A:PHE74 4.5 0.4 1.0 CA A:HIS96 4.5 0.3 1.0 CG1 A:VAL64 4.5 0.4 1.0 CB A:VAL64 4.6 0.3 1.0 HE1 A:PHE85 4.6 0.8 1.0 CB A:ASP70 4.7 0.6 1.0 HB A:VAL64 4.7 0.3 1.0 HB3 A:ASP70 4.8 1.2 1.0 HD1 A:HIS83 4.9 0.6 1.0 HA A:HIS96 4.9 0.3 1.0 HD1 A:HIS68 4.9 0.5 1.0

F.J.Moy, P.K.Chanda, J.M.Chen, S.Cosmi, W.Edris, J.S.Skotnicki, J.Wilhelm, R.Powers. uc(Nmr) Solution Structure of the Catalytic Fragment of Human Fibroblast Collagenase Complexed with A Sulfonamide Derivative of A Hydroxamic Acid Compound. Biochemistry V. 38 7085 1999.
ISSN: ISSN 0006-2960
PubMed: 10353819
DOI: 10.1021/BI982576V