Atomistry » Zinc » PDB 1mkm-1mxz » 1mp0
Atomistry »
  Zinc »
    PDB 1mkm-1mxz »
      1mp0 »

Zinc in PDB 1mp0: Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)

Enzymatic activity of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)

All present enzymatic activity of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H):
1.1.1.1; 1.2.1.1;

Protein crystallography data

The structure of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H), PDB code: 1mp0 was solved by P.C.Sanghani, H.Robinson, T.D.Hurley, W.F.Bosron, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.90 / 2.20
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.033, 79.033, 311.755, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 21.8

Other elements in 1mp0:

The structure of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) also contains other interesting chemical elements:

Potassium (K) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) (pdb code 1mp0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H), PDB code: 1mp0:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1mp0

Go back to Zinc Binding Sites List in 1mp0
Zinc binding site 1 out of 4 in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn375

b:37.6
occ:1.00
 SG A:CYS110 2.3 18.0 1.0
SG A:CYS102 2.4 20.7 1.0
SG A:CYS96 2.4 21.2 1.0
SG A:CYS99 2.4 21.8 1.0
CB A:CYS110 3.2 20.6 1.0
CB A:CYS102 3.4 21.9 1.0
CB A:CYS96 3.4 19.8 1.0
CB A:CYS99 3.4 25.5 1.0
N A:CYS96 3.5 19.0 1.0
CA A:CYS110 3.6 21.6 1.0
N A:CYS99 3.8 27.5 1.0
N A:GLY97 3.8 21.1 1.0
CA A:CYS96 3.9 20.3 1.0
N A:CYS102 4.2 22.4 1.0
CA A:CYS99 4.2 26.5 1.0
C A:CYS96 4.3 21.5 1.0
N A:GLN111 4.3 24.8 1.0
CA A:CYS102 4.3 21.6 1.0
N A:GLU98 4.4 26.2 1.0
C A:CYS110 4.4 22.5 1.0
CB A:LYS112 4.4 30.1 1.0
C A:GLN95 4.5 19.9 1.0
N A:LYS112 4.6 26.7 1.0
CA A:GLN95 4.8 19.1 1.0
CA A:GLY97 4.8 22.4 1.0
C A:CYS99 4.8 26.9 1.0
N A:CYS110 4.9 21.8 1.0
O A:CYS99 4.9 28.3 1.0
C A:GLU98 4.9 28.8 1.0

Zinc binding site 2 out of 4 in 1mp0

Go back to Zinc Binding Sites List in 1mp0
Zinc binding site 2 out of 4 in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn376

b:35.6
occ:1.00
 OE2 A:GLU67 2.1 16.7 1.0
NE2 A:HIS66 2.2 24.9 1.0
SG A:CYS44 2.3 21.4 1.0
SG A:CYS173 2.4 23.5 1.0
CD A:GLU67 3.1 17.2 1.0
CE1 A:HIS66 3.1 23.0 1.0
CD2 A:HIS66 3.2 22.5 1.0
CB A:CYS44 3.2 21.4 1.0
CB A:CYS173 3.2 17.2 1.0
CG A:GLU67 3.4 18.2 1.0
NH2 A:ARG368 3.6 17.4 1.0
O A:HOH815 3.7 31.2 1.0
NE A:ARG368 4.1 16.9 1.0
OE1 A:GLU67 4.2 16.2 1.0
OG1 A:THR46 4.2 23.2 1.0
ND1 A:HIS66 4.2 23.5 1.0
CG A:HIS66 4.2 21.4 1.0
CZ A:ARG368 4.3 19.4 1.0
CA A:CYS44 4.5 23.9 1.0
O A:HOH1108 4.6 41.2 1.0
CB A:THR46 4.6 23.7 1.0
N A:GLY174 4.7 20.3 1.0
CA A:CYS173 4.7 19.3 1.0
N A:CYS44 4.7 22.1 1.0
CB A:GLU67 4.8 19.4 1.0
O A:HOH824 5.0 10.8 1.0
O A:HOH817 5.0 17.8 1.0

Zinc binding site 3 out of 4 in 1mp0

Go back to Zinc Binding Sites List in 1mp0
Zinc binding site 3 out of 4 in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn375

b:33.3
occ:1.00
 SG B:CYS102 2.3 17.5 1.0
SG B:CYS110 2.4 15.2 1.0
SG B:CYS96 2.4 18.6 1.0
SG B:CYS99 2.4 18.9 1.0
CB B:CYS110 3.2 18.2 1.0
CB B:CYS102 3.4 18.2 1.0
N B:CYS96 3.4 15.7 1.0
CB B:CYS96 3.5 14.9 1.0
CB B:CYS99 3.5 21.2 1.0
CA B:CYS110 3.6 19.7 1.0
N B:CYS99 3.8 23.3 1.0
N B:GLY97 3.9 21.4 1.0
CA B:CYS96 3.9 19.0 1.0
N B:GLN111 4.2 22.5 1.0
CA B:CYS99 4.2 22.4 1.0
N B:CYS102 4.3 17.9 1.0
C B:CYS96 4.3 20.0 1.0
C B:CYS110 4.3 21.2 1.0
CA B:CYS102 4.4 17.7 1.0
CB B:LYS112 4.4 25.5 1.0
N B:GLU98 4.4 24.4 1.0
N B:LYS112 4.5 22.9 1.0
C B:GLN95 4.5 17.8 1.0
CA B:GLN95 4.8 17.4 1.0
CA B:GLY97 4.9 21.6 1.0
N B:CYS110 4.9 19.0 1.0
C B:CYS99 4.9 21.5 1.0
C B:GLU98 5.0 25.5 1.0

Zinc binding site 4 out of 4 in 1mp0

Go back to Zinc Binding Sites List in 1mp0
Zinc binding site 4 out of 4 in the Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Binary Complex of Human Glutathione-Dependent Formaldehyde Dehydrogenase with Nad(H) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn376

b:64.9
occ:1.00
 SG B:CYS44 2.2 36.5 1.0
OE2 B:GLU67 2.2 30.7 1.0
NE2 B:HIS66 2.5 26.9 1.0
SG B:CYS173 2.8 32.2 1.0
O B:HOH804 2.9 15.0 1.0
CB B:CYS44 3.0 33.9 1.0
CD B:GLU67 3.2 27.3 1.0
CE1 B:HIS66 3.2 26.2 1.0
CB B:CYS173 3.2 22.2 1.0
CD2 B:HIS66 3.5 25.1 1.0
CG B:GLU67 3.6 26.5 1.0
NH2 B:ARG368 3.7 22.7 1.0
OE1 B:GLU67 4.2 27.9 1.0
ND1 B:HIS66 4.3 23.6 1.0
O B:HOH990 4.4 46.2 1.0
CA B:CYS44 4.4 34.0 1.0
OG1 B:THR46 4.4 32.1 1.0
CG B:HIS66 4.5 22.6 1.0
N B:GLY174 4.5 20.4 1.0
CZ B:ARG368 4.5 24.6 1.0
NE B:ARG368 4.6 22.1 1.0
CA B:CYS173 4.6 21.2 1.0
CB B:THR46 4.7 29.5 1.0
N B:CYS44 4.8 29.8 1.0
C5N B:NAD778 4.9 19.1 1.0
C B:CYS44 5.0 34.5 1.0
C B:CYS173 5.0 19.6 1.0
CB B:GLU67 5.0 23.2 1.0

Reference:

P.C.Sanghani, H.Robinson, R.Bennett-Lovsey, T.D.Hurley, W.F.Bosron. Structure-Function Relationships in Human Class III Alcohol Dehydrogenase (Formaldehyde Dehydrogenase) Chem.Biol.Interact. V. 143 195 2003.
ISSN: ISSN 0009-2797
PubMed: 12604204
DOI: 10.1016/S0009-2797(02)00203-X
Page generated: Wed Oct 16 17:01:11 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy