Iron in PDB 5abn: Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi. Mutated Residues D69S, T70D, S86E, D146T, Q202L, H232E, Q239R and S301K.

Enzymatic activity of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi. Mutated Residues D69S, T70D, S86E, D146T, Q202L, H232E, Q239R and S301K.

Protein crystallography data

Other elements in 5abn:

Iron Binding Sites:

Iron binding site 1 out of 1 in 5abn

Iron Binding Sites List in 5abn

Iron binding site 1 out of 1 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi. Mutated Residues D69S, T70D, S86E, D146T, Q202L, H232E, Q239R and S301K.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii. Mutant Vpi. Mutated Residues D69S, T70D, S86E, D146T, Q202L, H232E, Q239R and S301K. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:36.7 occ:1.00 FE A:HEM500 0.0 36.7 1.0 NC A:HEM500 2.0 31.5 1.0 NA A:HEM500 2.0 30.4 1.0 ND A:HEM500 2.1 26.9 1.0 NB A:HEM500 2.2 39.8 1.0 NE2 A:HIS169 2.4 41.0 1.0 C1A A:HEM500 3.0 37.3 1.0 C4C A:HEM500 3.0 32.2 1.0 C4D A:HEM500 3.1 26.1 1.0 C1C A:HEM500 3.1 38.6 1.0 C1D A:HEM500 3.1 27.2 1.0 C4A A:HEM500 3.1 35.5 1.0 C1B A:HEM500 3.2 34.5 1.0 C4B A:HEM500 3.2 38.4 1.0 CD2 A:HIS169 3.3 46.4 1.0 CHA A:HEM500 3.4 29.3 1.0 CE1 A:HIS169 3.4 31.8 1.0 CHD A:HEM500 3.4 30.1 1.0 CHC A:HEM500 3.5 31.5 1.0 CHB A:HEM500 3.5 27.7 1.0 C2C A:HEM500 4.3 40.5 1.0 C3C A:HEM500 4.3 29.9 1.0 C2A A:HEM500 4.3 34.3 1.0 C3A A:HEM500 4.3 26.4 1.0 C3D A:HEM500 4.3 33.2 1.0 C2D A:HEM500 4.3 29.7 1.0 C2B A:HEM500 4.4 39.5 1.0 C3B A:HEM500 4.4 40.9 1.0 ND1 A:HIS169 4.5 39.1 1.0 CG A:HIS169 4.5 40.7 1.0 OG A:SER168 4.9 41.9 1.0 CE2 A:PHE186 4.9 37.6 1.0 CD2 A:PHE46 5.0 43.3 1.0

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