4mlq: Difference between revisions
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{{STRUCTURE_4mlq| PDB=4mlq | SCENE= }} | |||
===Crystal structure of Bacillus megaterium porphobilinogen deaminase=== | |||
{{ABSTRACT_PUBMED_24598743}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/Q8GCA8_BACME Q8GCA8_BACME]] Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps (By similarity).[HAMAP-Rule:MF_00260][SAAS:SAAS022418_004_010364] | |||
==About this Structure== | |||
[[4mlq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MLQ OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024598743</ref><references group="xtra"/><references/> | |||
[[Category: Hydroxymethylbilane synthase]] | |||
[[Category: Akhtar, M.]] | |||
[[Category: Azim, N.]] | |||
[[Category: Coker, A.]] | |||
[[Category: Cooper, J B.]] | |||
[[Category: Deery, E.]] | |||
[[Category: Erskine, P.]] | |||
[[Category: Warren, M J.]] | |||
[[Category: Wood, S P.]] | |||
[[Category: Dipyrromethane cofactor]] | |||
[[Category: Domains 1 and 2 resemble the fold of type ii periplasmic binding protein]] | |||
[[Category: Porphobilinogen deaminase]] | |||
[[Category: Pyrrole polymerisation]] | |||
[[Category: Tetrapyrrole biosynthesis]] | |||
[[Category: Three-domain fold]] | |||
[[Category: Transferase]] | |||
Revision as of 12:15, 2 April 2014
Crystal structure of Bacillus megaterium porphobilinogen deaminaseCrystal structure of Bacillus megaterium porphobilinogen deaminase
Template:ABSTRACT PUBMED 24598743
FunctionFunction
[Q8GCA8_BACME] Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps (By similarity).[HAMAP-Rule:MF_00260][SAAS:SAAS022418_004_010364]
About this StructureAbout this Structure
4mlq is a 1 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Azim N, Deery E, Warren MJ, Wolfenden BA, Erskine P, Cooper JB, Coker A, Wood SP, Akhtar M. Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):744-51. doi:, 10.1107/S139900471303294X. Epub 2014 Feb 15. PMID:24598743 doi:http://dx.doi.org/10.1107/S139900471303294X
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Hydroxymethylbilane synthase
- Akhtar, M.
- Azim, N.
- Coker, A.
- Cooper, J B.
- Deery, E.
- Erskine, P.
- Warren, M J.
- Wood, S P.
- Dipyrromethane cofactor
- Domains 1 and 2 resemble the fold of type ii periplasmic binding protein
- Porphobilinogen deaminase
- Pyrrole polymerisation
- Tetrapyrrole biosynthesis
- Three-domain fold
- Transferase