Enzyme

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EC Tree
     1. Oxidoreductases
        1.16 Oxidizing metal ions
            1.16.3 With oxygen as acceptor
ID:1.16.3.2
Description:Bacterial non-heme ferritin.
Cath: 1.20.1260.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.16.3.2
BRENDA Enzyme Link: BRENDA 1.16.3.2
KEGG Enzyme Link: KEGG1.16.3.2
BioCyc Enzyme Link: BioCyc 1.16.3.2
ExPASy Enzyme Link: ExPASy1.16.3.2
EC2PDB Enzyme Link: EC2PDB 1.16.3.2
ExplorEnz Enzyme Link: ExplorEnz 1.16.3.2
PRIAM enzyme-specific profiles Link: PRIAM 1.16.3.2
IntEnz Enzyme Link: IntEnz 1.16.3.2
MEDLINE Enzyme Link: MEDLINE 1.16.3.2
MSA:

1.16.3.2;

Phylogenetic Tree:

1.16.3.2;

Uniprot:
M-CSA:
RHEA:11972 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
RULE(radius=1) [Fe+2;H0:1].[Fe+2;H0:2].[O;H0;+0:3]=[O;H0;+0:4].[OH2;+0:5].[OH2;+0:6]>>[O;H0;+0:3]=[Fe;H0;+0:1]-[OH;+0:4].[O;H0;+0:6]=[Fe;H0;+0:2]-[OH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Functionality of the three-site ferroxidase center of Escherichia coli bacterial ferritin (EcFtnA).Bou-Abdallah F, Yang H, Awomolo A, Cooper B, Woodhall MR, Andrews SC, Chasteen ND2014 Jan 2824380371
The high-resolution X-ray crystallographic structure of the ferritin (EcFtnA) of Escherichia coli; comparison with human H ferritin (HuHF) and the structures of the Fe(3+) and Zn(2+) derivatives.Stillman TJ, Hempstead PD, Artymiuk PJ, Andrews SC, Hudson AJ, Treffry A, Guest JR, Harrison PM2001 Mar 2311254384