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Iron in PDB 5y5g: Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray

Enzymatic activity of Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray

All present enzymatic activity of Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray:
1.7.1.14;

Protein crystallography data

The structure of Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray, PDB code: 5y5g was solved by T.Tosha, T.Nomura, T.Nishida, G.Ueno, H.Murakami, K.Yamashita, K.Hirata, M.Yamamoto, H.Ago, H.Sugimoto, Y.Shiro, M.Kubo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.97 / 1.36
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.189, 75.477, 101.668, 90.00, 90.00, 90.00
R / Rfree (%) 13.3 / 16.6

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray (pdb code 5y5g). 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 Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray, PDB code: 5y5g:

Iron binding site 1 out of 1 in 5y5g

Go back to Iron Binding Sites List in 5y5g
Iron binding site 1 out of 1 in the Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Cytochrome P450NOR in No-Bound State: Damaged By Low-Dose (0.72 Mgy) X-Ray within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:10.9
occ:1.00
FE A:HEM501 0.0 10.9 1.0
NA A:HEM501 2.0 10.3 1.0
NB A:HEM501 2.0 10.2 1.0
ND A:HEM501 2.0 11.1 1.0
NC A:HEM501 2.0 10.3 1.0
N A:NO502 2.1 16.1 1.0
SG A:CYS352 2.3 11.0 1.0
C1A A:HEM501 3.0 9.9 1.0
C4A A:HEM501 3.0 10.3 1.0
C4D A:HEM501 3.0 10.7 1.0
C1B A:HEM501 3.0 10.2 1.0
C4B A:HEM501 3.1 10.0 1.0
C1D A:HEM501 3.1 10.5 1.0
C4C A:HEM501 3.1 10.4 1.0
O A:NO502 3.1 19.4 1.0
C1C A:HEM501 3.1 10.0 1.0
HB2 A:CYS352 3.3 12.6 1.0
CHA A:HEM501 3.4 10.4 1.0
CHB A:HEM501 3.4 10.5 1.0
CHD A:HEM501 3.4 10.3 1.0
CB A:CYS352 3.4 10.5 1.0
CHC A:HEM501 3.4 9.6 1.0
HA A:CYS352 3.8 12.3 1.0
HB3 A:CYS352 4.2 12.6 1.0
C2A A:HEM501 4.2 11.0 1.0
CA A:CYS352 4.2 10.2 1.0
C3A A:HEM501 4.2 10.8 1.0
C3D A:HEM501 4.3 11.2 1.0
C2D A:HEM501 4.3 10.7 1.0
C3B A:HEM501 4.3 10.4 1.0
C2B A:HEM501 4.3 11.0 1.0
C3C A:HEM501 4.3 10.9 1.0
C2C A:HEM501 4.3 10.9 1.0
HHA A:HEM501 4.4 12.4 1.0
HHB A:HEM501 4.4 12.6 1.0
HHD A:HEM501 4.4 12.3 1.0
HHC A:HEM501 4.4 11.5 1.0
O A:HOH945 4.7 30.4 1.0
CA A:GLY240 4.8 11.7 1.0
O A:HOH1164 4.8 51.8 1.0
O A:ALA239 4.9 14.2 1.0

Reference:

T.Tosha, T.Nomura, T.Nishida, N.Saeki, K.Okubayashi, R.Yamagiwa, M.Sugahara, T.Nakane, K.Yamashita, K.Hirata, G.Ueno, T.Kimura, T.Hisano, K.Muramoto, H.Sawai, H.Takeda, E.Mizohata, A.Yamashita, Y.Kanematsu, Y.Takano, E.Nango, R.Tanaka, O.Nureki, O.Shoji, Y.Ikemoto, H.Murakami, S.Owada, K.Tono, M.Yabashi, M.Yamamoto, H.Ago, S.Iwata, H.Sugimoto, Y.Shiro, M.Kubo. Capturing An Initial Intermediate During the P450NOR Enzymatic Reaction Using Time-Resolved Xfel Crystallography and Caged-Substrate. Nat Commun V. 8 1585 2017.
ISSN: ESSN 2041-1723
PubMed: 29147002
DOI: 10.1038/S41467-017-01702-1
Page generated: Sun Dec 13 16:18:16 2020

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