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Zinc in PDB 2rhq: Phers From Staphylococcus Haemolyticus- Rational Protein Engineering and Inhibitor Studies

Enzymatic activity of Phers From Staphylococcus Haemolyticus- Rational Protein Engineering and Inhibitor Studies

All present enzymatic activity of Phers From Staphylococcus Haemolyticus- Rational Protein Engineering and Inhibitor Studies:
6.1.1.20;

Protein crystallography data

The structure of Phers From Staphylococcus Haemolyticus- Rational Protein Engineering and Inhibitor Studies, PDB code: 2rhq was solved by A.G.Evdokimov, M.Mekel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.60 / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 249.312, 87.602, 61.072, 90.00, 100.44, 90.00
R / Rfree (%) 19.6 / 26.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Phers From Staphylococcus Haemolyticus- Rational Protein Engineering and Inhibitor Studies (pdb code 2rhq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Phers From Staphylococcus Haemolyticus- Rational Protein Engineering and Inhibitor Studies, PDB code: 2rhq:

Zinc binding site 1 out of 1 in 2rhq

Go back to Zinc Binding Sites List in 2rhq
Zinc binding site 1 out of 1 in the Phers From Staphylococcus Haemolyticus- Rational Protein Engineering and Inhibitor Studies


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Phers From Staphylococcus Haemolyticus- Rational Protein Engineering and Inhibitor Studies within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1

b:57.1
occ:1.00
 SG A:CYS278 2.3 54.1 1.0
SG A:CYS270 2.3 56.3 1.0
SG A:CYS275 2.3 56.9 1.0
SG A:CYS267 2.4 51.8 1.0
CB A:CYS267 3.3 50.6 1.0
CB A:CYS275 3.3 59.7 1.0
CB A:CYS270 3.3 65.0 1.0
N A:CYS275 3.4 58.0 1.0
CB A:CYS278 3.4 52.8 1.0
CA A:CYS275 3.8 59.5 1.0
C A:GLY274 3.9 60.4 1.0
N A:CYS278 4.0 52.0 1.0
N A:CYS270 4.1 65.2 1.0
CA A:GLY274 4.2 66.5 1.0
CA A:CYS278 4.3 51.9 1.0
CA A:CYS270 4.3 65.2 1.0
C A:CYS275 4.4 59.6 1.0
O A:CYS275 4.5 58.1 1.0
CB A:VAL277 4.6 59.4 1.0
O A:GLY274 4.6 57.4 1.0
CB A:LYS269 4.6 62.7 1.0
N A:GLY274 4.6 70.8 1.0
CA A:CYS267 4.7 50.3 1.0
CA A:GLY282 4.7 51.7 1.0
C A:LYS269 4.9 66.5 1.0
C A:VAL277 4.9 55.6 1.0

Reference:

A.G.Evdokimov, M.Mekel, K.Hutchings, L.Narasimhan, T.Holler, T.Mcgrath, B.Beattie, E.Fauman, C.Yan, H.Heaslet, R.Walter, B.Finzel, J.Ohren, P.Mcconnell, T.Braden, F.Sun, C.Spessard, C.Banotai, L.Al-Kassim, W.Ma, P.Wengender, D.Kole, N.Garceau, P.Toogood, J.Liu. Rational Protein Engineering in Action: the First Crystal Structure of A Phenylalanine Trna Synthetase From Staphylococcus Haemolyticus. J.Struct.Biol. V. 162 152 2008.
ISSN: ISSN 1047-8477
PubMed: 18086534
DOI: 10.1016/J.JSB.2007.11.002
Page generated: Thu Oct 17 03:49:11 2024

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