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Zinc in PDB 4axq: Crystal Structure of Archaemetzincin (Amza) From Archaeoglobus Fulgidus at 1.4 A Resolution

Protein crystallography data

The structure of Crystal Structure of Archaemetzincin (Amza) From Archaeoglobus Fulgidus at 1.4 A Resolution, PDB code: 4axq was solved by C.Graef, M.Schacherl, U.Baumann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.409 / 1.40
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 88.339, 88.339, 50.275, 90.00, 90.00, 90.00
R / Rfree (%) 16.41 / 18.64

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Archaemetzincin (Amza) From Archaeoglobus Fulgidus at 1.4 A Resolution (pdb code 4axq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Archaemetzincin (Amza) From Archaeoglobus Fulgidus at 1.4 A Resolution, PDB code: 4axq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4axq

Go back to Zinc Binding Sites List in 4axq
Zinc binding site 1 out of 2 in the Crystal Structure of Archaemetzincin (Amza) From Archaeoglobus Fulgidus at 1.4 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Archaemetzincin (Amza) From Archaeoglobus Fulgidus at 1.4 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1161

b:14.8
occ:1.00
SG A:CYS154 2.3 14.6 1.0
SG A:CYS132 2.3 12.5 1.0
SG A:CYS128 2.3 17.6 1.0
SG A:CYS151 2.4 14.9 1.0
HB2 A:CYS132 3.0 18.3 1.0
HB2 A:CYS128 3.0 19.9 1.0
HB2 A:CYS154 3.1 16.6 1.0
CB A:CYS128 3.1 16.6 1.0
CB A:CYS132 3.1 15.2 1.0
HB3 A:CYS151 3.3 18.1 1.0
HB3 A:CYS128 3.3 19.9 1.0
H A:CYS151 3.3 16.7 1.0
CB A:CYS154 3.3 13.9 1.0
HB3 A:CYS132 3.3 18.3 1.0
CB A:CYS151 3.4 15.0 1.0
H A:CYS154 3.5 17.1 1.0
HB2 A:ASN130 3.6 26.4 1.0
HB2 A:MET134 3.6 12.2 1.0
HD21 A:ASN130 3.8 27.6 1.0
N A:CYS151 4.0 13.9 1.0
HB3 A:CYS154 4.0 16.6 1.0
N A:CYS154 4.1 14.2 1.0
O A:HOH2239 4.1 23.5 1.0
HB2 A:CYS151 4.2 18.1 1.0
HB2 A:GLU153 4.2 20.1 1.0
CA A:CYS151 4.2 13.9 1.0
CA A:CYS154 4.3 13.9 1.0
H A:MET134 4.4 12.6 1.0
O A:HOH2271 4.5 24.7 1.0
H A:ASN130 4.5 26.1 1.0
CB A:MET134 4.5 10.2 1.0
CB A:ASN130 4.6 22.0 1.0
ND2 A:ASN130 4.6 23.0 1.0
CA A:CYS128 4.6 17.2 1.0
CA A:CYS132 4.6 12.2 1.0
HG2 A:MET134 4.7 12.4 1.0
HA A:CYS154 4.7 16.7 1.0
HA A:PHE150 4.7 15.9 1.0
HA A:CYS132 4.8 14.6 1.0
C A:CYS151 4.8 14.7 1.0
HG3 A:MET134 4.8 12.4 1.0
HA A:CYS128 4.8 20.7 1.0
HD1 A:PHE150 4.9 14.2 1.0
O A:CYS151 4.9 14.0 1.0
O A:HOH2234 4.9 19.7 1.0
HB3 A:ASN130 5.0 26.4 1.0
CG A:MET134 5.0 10.3 1.0

Zinc binding site 2 out of 2 in 4axq

Go back to Zinc Binding Sites List in 4axq
Zinc binding site 2 out of 2 in the Crystal Structure of Archaemetzincin (Amza) From Archaeoglobus Fulgidus at 1.4 A Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Archaemetzincin (Amza) From Archaeoglobus Fulgidus at 1.4 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1162

b:12.3
occ:1.00
NE2 A:HIS127 2.1 14.9 1.0
NE2 A:HIS117 2.1 9.3 1.0
NE2 A:HIS121 2.2 10.2 1.0
CE1 A:HIS127 3.0 15.8 1.0
CD2 A:HIS117 3.1 7.9 1.0
CE1 A:HIS117 3.1 10.4 1.0
CD2 A:HIS127 3.1 14.4 1.0
CE1 A:HIS121 3.1 11.4 1.0
CD2 A:HIS121 3.2 10.3 1.0
HE1 A:HIS127 3.2 19.0 1.0
HD2 A:HIS117 3.2 9.5 1.0
HE1 A:HIS117 3.3 12.5 1.0
HE1 A:HIS121 3.3 13.7 1.0
HD2 A:HIS121 3.3 12.4 1.0
HD2 A:HIS127 3.3 17.2 1.0
HA A:PHE136 4.2 33.7 1.0
ND1 A:HIS127 4.2 16.5 1.0
ND1 A:HIS117 4.2 9.6 1.0
O A:HOH2228 4.2 19.7 1.0
CG A:HIS117 4.2 8.5 1.0
CG A:HIS127 4.2 15.5 1.0
ND1 A:HIS121 4.3 11.4 1.0
CG A:HIS121 4.3 9.9 1.0
H A:SER137 4.7 30.9 1.0
HE2 A:MET134 4.7 13.3 1.0
HE1 A:MET134 4.7 13.3 1.0
OE1 A:GLU118 4.9 13.5 1.0
HD1 A:HIS127 4.9 19.8 1.0
HD1 A:HIS117 5.0 11.5 1.0

Reference:

C.Graef, M.Schacherl, S.Waltersperger, U.Baumann. Crystal Structures of Archaemetzincin Reveal A Moldable Substrate-Binding Site. Plos One V. 7 43863 2012.
ISSN: ISSN 1932-6203
PubMed: 22937112
DOI: 10.1371/JOURNAL.PONE.0043863
Page generated: Wed Aug 20 16:02:55 2025

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