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Iron in PDB 5y5h: Sf-Rox Structure of Cytochrome P450NOR (No-Bound State) Determined at Sacla

Enzymatic activity of Sf-Rox Structure of Cytochrome P450NOR (No-Bound State) Determined at Sacla

All present enzymatic activity of Sf-Rox Structure of Cytochrome P450NOR (No-Bound State) Determined at Sacla:
1.7.1.14;

Protein crystallography data

The structure of Sf-Rox Structure of Cytochrome P450NOR (No-Bound State) Determined at Sacla, PDB code: 5y5h was solved by T.Tosha, T.Nomura, T.Nishida, R.Yamagiwa, K.Yamashita, K.Hirata, G.Ueno, T.Kimura, T.Hisano, K.Muramoto, H.Sawai, H.Takeda, A.Yamashita, H.Murakami, S.Owada, K.Tono, M.Yabashi, 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) 24.45 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.017, 75.570, 101.760, 90.00, 90.00, 90.00
R / Rfree (%) 16.9 / 19.6

Iron Binding Sites:

The binding sites of Iron atom in the Sf-Rox Structure of Cytochrome P450NOR (No-Bound State) Determined at Sacla (pdb code 5y5h). 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 Sf-Rox Structure of Cytochrome P450NOR (No-Bound State) Determined at Sacla, PDB code: 5y5h:

Iron binding site 1 out of 1 in 5y5h

Go back to Iron Binding Sites List in 5y5h
Iron binding site 1 out of 1 in the Sf-Rox Structure of Cytochrome P450NOR (No-Bound State) Determined at Sacla


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sf-Rox Structure of Cytochrome P450NOR (No-Bound State) Determined at Sacla within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:21.8
occ:1.00
FE A:HEM501 0.0 21.8 1.0
N A:NO502 1.7 23.6 1.0
NA A:HEM501 2.0 22.2 1.0
ND A:HEM501 2.0 19.1 1.0
NB A:HEM501 2.0 20.3 1.0
NC A:HEM501 2.1 20.9 1.0
SG A:CYS352 2.3 19.9 1.0
O A:NO502 2.8 25.6 1.0
C1A A:HEM501 3.0 21.7 1.0
C4A A:HEM501 3.0 20.9 1.0
C4D A:HEM501 3.0 20.9 1.0
C1D A:HEM501 3.0 19.6 1.0
C4C A:HEM501 3.1 19.7 1.0
C4B A:HEM501 3.1 21.9 1.0
C1C A:HEM501 3.1 22.3 1.0
C1B A:HEM501 3.1 21.8 1.0
HB2 A:CYS352 3.3 25.5 1.0
CHA A:HEM501 3.4 21.6 1.0
CHD A:HEM501 3.4 21.0 1.0
CHB A:HEM501 3.4 20.3 1.0
CB A:CYS352 3.4 21.3 1.0
CHC A:HEM501 3.4 20.9 1.0
HA A:CYS352 4.0 25.3 1.0
HB3 A:CYS352 4.2 25.5 1.0
C2A A:HEM501 4.2 22.1 1.0
C3A A:HEM501 4.2 18.8 1.0
C3D A:HEM501 4.2 22.2 1.0
C2D A:HEM501 4.3 21.2 1.0
C3C A:HEM501 4.3 21.7 1.0
C3B A:HEM501 4.3 22.1 1.0
C2C A:HEM501 4.3 20.7 1.0
C2B A:HEM501 4.3 22.1 1.0
CA A:CYS352 4.3 21.1 1.0
HHA A:HEM501 4.4 25.9 1.0
HHD A:HEM501 4.4 25.2 1.0
HHB A:HEM501 4.4 24.4 1.0
HHC A:HEM501 4.4 25.1 1.0
CA A:GLY240 4.7 21.5 1.0
O A:HOH716 4.7 30.7 1.0
O A:ALA239 4.8 22.4 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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