This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2mad
From Proteopedia
| |||||||||
| 2mad, resolution 2.25Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Non-Standard Residues: | |||||||||
| Activity: | Amine dehydrogenase, with EC number 1.4.99.3 | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
THE ACTIVE SITE STRUCTURE OF METHYLAMINE DEHYDROGENASE: HYDRAZINES IDENTIFY C6 AS THE REACTIVE SITE OF THE TRYPTOPHAN DERIVED QUINONE COFACTOR
Template:ABSTRACT PUBMED 1390754
About this Structure
2mad is a 2 chain structure with sequence from Paracoccus versutus. This structure supersedes the now removed PDB entry 1mad. Full crystallographic information is available from OCA.
See Also
Reference
- Huizinga EG, van Zanten BA, Duine JA, Jongejan JA, Huitema F, Wilson KS, Hol WG. Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor. Biochemistry. 1992 Oct 13;31(40):9789-95. PMID:1390754
