2BT3: AGAO in complex with Ruthenium-C4-wire at 1.73 angstroms

Citation:
Abstract
Molecular wires comprising a Ru(II)- or Re(I)-complex head group, an aromatic tail group, and an alkane linker reversibly inhibit the activity of the copper amine oxidase from Arthrobacter globiformis (AGAO), with K(i) values between 6 muM and 37 nM. In the crystal structure of a Ru(II)-wire:AGAO conjugate, the wire occupies the AGAO active-site substrate access channel, the trihydroxyphenylalanine quinone cofactor is ordered in the "off-Cu" position with its reactive carbonyl oriented toward the inhibitor, and the "gate" residue, Tyr-296, is in the "open" position. Head groups, tail-group substituents, and linker lengths all influence wire-binding interactions with the enzyme.
PDB ID: 2BT3Download
MMDB ID: 38453
PDB Deposition Date: 2005/5/26
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 1.73  Å
Source Organism:
Similar Structures:
Biological Unit for 2BT3: dimeric; determined by author and by software (PQS)
Molecular Components in 2BT3
Label Count Molecule
Proteins (2 molecules)
2
Phenylethylamine Oxidase
Molecule annotation
Chemicals (24 molecules)
1
2
2
2
3
2
4
6
5
12
* Click molecule labels to explore molecular sequence information.

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