Atomistry » Iron » PDB 2v1j-2vlz » 2vbp
Atomistry »
  Iron »
    PDB 2v1j-2vlz »
      2vbp »

Iron in PDB 2vbp: Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed)

Enzymatic activity of Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed)

All present enzymatic activity of Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed):
1.21.3.1;

Protein crystallography data

The structure of Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed), PDB code: 2vbp was solved by W.Ge, I.J.Clifton, R.M.Adlington, J.E.Baldwin, P.J.Rutledge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 59.76 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.515, 74.340, 100.704, 90.00, 90.00, 90.00
R / Rfree (%) 14.7 / 18.1

Iron Binding Sites:

The binding sites of Iron atom in the Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed) (pdb code 2vbp). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed), PDB code: 2vbp:

Iron binding site 1 out of 1 in 2vbp

Go back to Iron Binding Sites List in 2vbp
Iron binding site 1 out of 1 in the Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Isopenicillin N Synthase with Substrate Analogue L,L,L-Acab (Unexposed) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1332

b:9.7
occ:1.00
O A:HOH2319 2.1 11.1 1.0
OD1 A:ASP216 2.2 10.8 1.0
O A:HOH2436 2.2 12.3 1.0
NE2 A:HIS270 2.2 8.0 1.0
NE2 A:HIS214 2.2 9.8 1.0
S17 A:VB11333 2.4 15.0 1.0
CE1 A:HIS270 3.1 8.9 1.0
CG A:ASP216 3.1 11.1 1.0
CE1 A:HIS214 3.2 10.6 1.0
CD2 A:HIS270 3.2 7.5 1.0
CD2 A:HIS214 3.2 9.3 1.0
C16 A:VB11333 3.4 19.2 1.0
OD2 A:ASP216 3.5 10.2 1.0
O A:HOH2001 3.9 25.8 1.0
O A:HOH2002 4.2 30.9 1.0
ND1 A:HIS270 4.3 8.2 1.0
O A:HOH2363 4.3 12.7 1.0
ND1 A:HIS214 4.3 9.6 1.0
CG A:HIS270 4.3 7.2 1.0
CG A:HIS214 4.4 10.4 1.0
O42 A:VB11333 4.4 31.2 1.0
CB A:ASP216 4.5 8.4 1.0
O A:HOH2320 4.7 16.4 1.0
CA A:ASP216 4.8 8.7 1.0
C12 A:VB11333 4.9 18.4 1.0

Reference:

W.Ge, I.J.Clifton, J.E.Stok, R.M.Adlington, J.E.Baldwin, P.J.Rutledge. Crystallographic Studies on the Binding of Selectively Deuterated Lld- and Lll-Substrate Epimers By Isopenicillin N Synthase. Biochem.Biophys.Res.Commun. V. 398 659 2010.
ISSN: ISSN 0006-291X
PubMed: 20603104
DOI: 10.1016/J.BBRC.2010.06.129
Page generated: Sun Dec 13 14:53:39 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy