Zinc in PDB 7sek: Solution Structure of the Zinc Finger Domain of Murine METAP1, Complexed with Zng N-Terminal Peptide

Enzymatic activity of Solution Structure of the Zinc Finger Domain of Murine METAP1, Complexed with Zng N-Terminal Peptide

All present enzymatic activity of Solution Structure of the Zinc Finger Domain of Murine METAP1, Complexed with Zng N-Terminal Peptide:
3.4.11.18;

Zinc Binding Sites:

The binding sites of Zinc atom in the Solution Structure of the Zinc Finger Domain of Murine METAP1, Complexed with Zng N-Terminal Peptide (pdb code 7sek). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of the Zinc Finger Domain of Murine METAP1, Complexed with Zng N-Terminal Peptide, PDB code: 7sek:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 7sek

Go back to Zinc Binding Sites List in 7sek
Zinc binding site 1 out of 2 in the Solution Structure of the Zinc Finger Domain of Murine METAP1, Complexed with Zng N-Terminal Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Zinc Finger Domain of Murine METAP1, Complexed with Zng N-Terminal Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn101

b:0.3
occ:1.00
SG A:CYS30 2.3 65.0 1.0
SG A:CYS57 2.4 22.4 1.0
SG A:CYS35 2.4 42.4 1.0
SG A:CYS61 2.4 51.3 1.0
HB2 A:CYS30 3.0 12.5 1.0
CB A:CYS30 3.1 32.0 1.0
H A:CYS57 3.2 34.4 1.0
HB3 A:CYS30 3.3 12.3 1.0
HB3 A:CYS57 3.4 64.3 1.0
HB3 A:CYS61 3.4 72.3 1.0
HB3 A:CYS35 3.4 32.1 1.0
CB A:CYS61 3.5 42.3 1.0
CB A:CYS35 3.5 61.0 1.0
CB A:CYS57 3.5 25.0 1.0
HB3 A:SER37 3.6 62.4 1.0
HB2 A:CYS61 3.7 34.2 1.0
HB2 A:CYS35 3.8 75.0 1.0
N A:CYS57 4.0 51.3 1.0
H A:SER58 4.1 74.1 1.0
HD1 A:PHE56 4.2 35.4 1.0
OG1 A:THR32 4.3 1.3 1.0
CA A:CYS57 4.3 54.4 1.0
HB2 A:CYS57 4.3 31.4 1.0
HB A:THR32 4.5 34.3 1.0
CA A:CYS30 4.5 23.5 1.0
CB A:SER37 4.5 31.3 1.0
HB2 A:SER37 4.6 34.4 1.0
H A:SER37 4.6 45.1 1.0
HA A:PHE56 4.6 42.4 1.0
HA A:CYS30 4.7 60.4 1.0
N A:SER58 4.8 43.1 1.0
CA A:CYS35 4.9 11.1 1.0
CA A:CYS61 4.9 3.5 1.0
HB3 A:PHE56 4.9 1.1 1.0
H A:THR32 4.9 4.3 1.0
OG A:SER58 5.0 24.2 1.0

Zinc binding site 2 out of 2 in 7sek

Go back to Zinc Binding Sites List in 7sek
Zinc binding site 2 out of 2 in the Solution Structure of the Zinc Finger Domain of Murine METAP1, Complexed with Zng N-Terminal Peptide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of the Zinc Finger Domain of Murine METAP1, Complexed with Zng N-Terminal Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn102

b:63.4
occ:1.00
NE2 A:HIS69 2.2 55.1 1.0
NE2 A:HIS73 2.2 62.4 1.0
SG A:CYS43 2.3 62.2 1.0
SG A:CYS46 2.5 3.1 1.0
CD2 A:HIS69 2.8 1.1 1.0
HD2 A:HIS69 2.8 65.2 1.0
HB3 A:CYS43 3.0 61.0 1.0
CB A:CYS43 3.1 0.3 1.0
CE1 A:HIS73 3.2 25.6 1.0
CD2 A:HIS73 3.2 14.4 1.0
HB2 A:CYS43 3.2 41.5 1.0
CE1 A:HIS69 3.3 24.1 1.0
HE1 A:HIS73 3.4 74.1 1.0
HB2 A:CYS46 3.4 54.1 1.0
HD2 A:HIS73 3.4 2.4 1.0
CB A:CYS46 3.5 33.1 1.0
HB3 A:SER54 3.6 3.0 1.0
HE1 A:HIS69 3.8 20.0 1.0
H A:CYS46 3.8 62.4 1.0
CG A:HIS69 3.9 62.1 1.0
HZ3 A:TRP66 3.9 24.4 1.0
HB A:THR45 4.0 74.5 1.0
N A:CYS46 4.1 35.5 1.0
HA A:CYS46 4.1 25.1 1.0
ND1 A:HIS69 4.2 31.0 1.0
CA A:CYS46 4.2 35.0 1.0
ND1 A:HIS73 4.3 74.5 1.0
HE2 A:PHE56 4.3 22.2 1.0
CG A:HIS73 4.3 32.2 1.0
HB3 A:CYS46 4.4 22.1 1.0
CA A:CYS43 4.5 11.5 1.0
HD11 A:ILE51 4.5 15.4 1.0
HD12 A:ILE51 4.6 31.4 1.0
CB A:SER54 4.6 61.4 1.0
CZ3 A:TRP66 4.8 73.4 1.0
C A:THR45 4.9 42.2 1.0
OG A:SER54 4.9 3.0 1.0
HA A:CYS43 4.9 2.2 1.0
HD11 A:LEU49 5.0 44.2 1.0
HB2 A:SER54 5.0 15.0 1.0

Reference:

A.Weiss, C.C.Murdoch, K.A.Edmonds, M.R.Jordan, A.J.Monteith, Y.R.Perera, A.M.Rodriguez Nassif, A.M.Petoletti, W.N.Beavers, M.J.Munneke, S.L.Drury, E.S.Krystofiak, K.Thalluri, H.Wu, A.R.S.Kruse, R.D.Dimarchi, R.M.Caprioli, J.M.Spraggins, W.J.Chazin, D.P.Giedroc, E.P.Skaar. Zn-Regulated Gtpase Metalloprotein Activator 1 Modulates Vertebrate Zinc Homeostasis. Cell V. 185 2148 2022.
ISSN: ISSN 1097-4172
PubMed: 35584702
DOI: 10.1016/J.CELL.2022.04.011
Page generated: Wed Oct 30 10:41:50 2024

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