4bta
From Proteopedia
(Difference between revisions)
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{{STRUCTURE_4bta| PDB=4bta | SCENE= }} | {{STRUCTURE_4bta| PDB=4bta | SCENE= }} | ||
===CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN=== | ===CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN=== | ||
| + | {{ABSTRACT_PUBMED_24207127}} | ||
==Function== | ==Function== | ||
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==About this Structure== | ==About this Structure== | ||
| - | [[4bta]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[4bta]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BTA OCA]. |
| - | [[Category: | + | |
| + | ==Reference== | ||
| + | <ref group="xtra">PMID:024207127</ref><references group="xtra"/><references/> | ||
| + | [[Category: Human]] | ||
[[Category: Procollagen-proline dioxygenase]] | [[Category: Procollagen-proline dioxygenase]] | ||
[[Category: Anantharajan, J.]] | [[Category: Anantharajan, J.]] | ||
Revision as of 12:26, 20 November 2013
Contents |
CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN
Template:ABSTRACT PUBMED 24207127
Function
[P4HA1_HUMAN] Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
About this Structure
4bta is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA.
Reference
- Anantharajan J, Koski MK, Kursula P, Hieta R, Bergmann U, Myllyharju J, Wierenga RK. The Structural Motifs for Substrate Binding and Dimerization of the alpha Subunit of Collagen Prolyl 4-Hydroxylase. Structure. 2013 Oct 23. pii: S0969-2126(13)00355-9. doi:, 10.1016/j.str.2013.09.005. PMID:24207127 doi:http://dx.doi.org/10.1016/j.str.2013.09.005
