Atomistry » Iron » PDB 2v1j-2vlz » 2ve1
Atomistry »
  Iron »
    PDB 2v1j-2vlz »
      2ve1 »

Iron in PDB 2ve1: Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR)

Enzymatic activity of Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR)

All present enzymatic activity of Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR):
1.21.3.1;

Protein crystallography data

The structure of Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR), PDB code: 2ve1 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) 60.75 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.672, 75.717, 101.910, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 24.6

Iron Binding Sites:

The binding sites of Iron atom in the Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR) (pdb code 2ve1). 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 Asmcov (Oxygen Exposed 1MIN 20BAR), PDB code: 2ve1:

Iron binding site 1 out of 1 in 2ve1

Go back to Iron Binding Sites List in 2ve1
Iron binding site 1 out of 1 in the Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR)


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 Asmcov (Oxygen Exposed 1MIN 20BAR) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:6.2
occ:1.00
OD1 A:ASP216 2.0 4.2 1.0
O A:HOH555 2.2 6.2 1.0
NE2 A:HIS270 2.2 2.8 1.0
NE2 A:HIS214 2.3 3.4 1.0
O31 A:W2X402 2.3 18.4 0.5
S17 A:M11403 2.4 19.8 0.5
S17 A:W2X402 2.5 6.0 0.5
C33 A:M11403 2.7 13.7 0.5
CG A:ASP216 3.1 3.9 1.0
CD2 A:HIS214 3.2 3.6 1.0
CD2 A:HIS270 3.2 2.9 1.0
CE1 A:HIS270 3.2 3.2 1.0
CE1 A:HIS214 3.3 3.6 1.0
C37 A:W2X402 3.4 19.5 0.5
C32 A:W2X402 3.4 20.1 0.5
C32 A:M11403 3.5 25.2 0.5
OD2 A:ASP216 3.5 5.0 1.0
C33 A:W2X402 3.6 21.9 0.5
C16 A:W2X402 3.7 13.3 0.5
CAV A:M11403 3.9 26.4 0.5
C25 A:W2X402 4.1 13.3 0.5
C25 A:M11403 4.2 27.8 0.5
ND1 A:HIS270 4.3 3.0 1.0
CG A:HIS270 4.3 3.0 1.0
CG A:HIS214 4.3 3.9 1.0
ND1 A:HIS214 4.4 3.9 1.0
C37 A:M11403 4.4 24.9 0.5
CB A:ASP216 4.4 3.6 1.0
O29 A:M11403 4.4 25.4 0.5
C30 A:M11403 4.6 24.6 0.5
CA A:ASP216 4.7 3.2 1.0
C13 A:M11403 4.8 25.2 0.5
C30 A:W2X402 4.9 18.7 0.5
C12 A:W2X402 4.9 12.9 0.5
C12 A:M11403 4.9 23.7 0.5
N A:ASP216 4.9 4.6 1.0
O A:HOH610 4.9 16.9 1.0

Reference:

W.Ge, I.J.Clifton, A.R.Howard-Jones, J.E.Stok, R.M.Adlington, J.E.Baldwin, P.J.Rutledge. Structural Studies on the Reaction of Isopenicillin N Synthase with A Sterically Demanding Depsipeptide Substrate Analogue. Chembiochem V. 10 2025 2009.
ISSN: ISSN 1439-4227
PubMed: 19598184
DOI: 10.1002/CBIC.200900080
Page generated: Sun Dec 13 14:53:44 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