Rea1 Wild type ADP state (tail part). Determined by electron microscopy at 3.9 Å resolution. Released 12 Dec 2018.
Explore 6HYD in 3D Show helices and sheets RCSB PDB PDBe
6HYD contains 94 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2359-2362 | 4 | |
| α-helix | 2369-2372 | 4 | |
| α-helix | 2376-2380 | 5 | |
| α-helix | 2391-2404 | 14 | |
| α-helix | 2407-2411 | 5 | |
| α-helix | 2416-2425 | 10 | |
| α-helix | 2447-2450 | 4 | |
| α-helix | 2463-2486 | 24 | |
| α-helix | 2496-2499 | 4 | |
| α-helix | 2523-2531 | 9 | |
| α-helix | 2543-2546 | 4 | |
| α-helix | 2550-2559 | 10 | |
| α-helix | 2566-2570 | 5 | |
| α-helix | 2572-2575 | 4 | |
| α-helix | 2578-2583 | 6 | |
| α-helix | 2591-2594 | 4 | |
| α-helix | 2601-2605 | 5 | |
| α-helix | 2613-2616 | 4 | |
| α-helix | 2628-2648 | 21 | |
| α-helix | 2659-2673 | 15 | |
| α-helix | 2681-2699 | 19 | |
| α-helix | 2705-2707 | 3 | |
| α-helix | 2711-2719 | 9 | |
| α-helix | 2727-2732 | 6 | |
| α-helix | 2741-2744 | 4 | |
| α-helix | 2758-2761 | 4 | |
| α-helix | 2780-2790 | 11 | |
| α-helix | 2807-2814 | 8 | |
| α-helix | 2818-2822 | 5 | |
| α-helix | 2831-2837 | 7 | |
| α-helix | 2840-2844 | 5 | |
| α-helix | 2854-2859 | 6 | |
| α-helix | 2861-2864 | 4 | |
| α-helix | 2869-2872 | 4 | |
| α-helix | 2873-2877 | 5 | |
| α-helix | 2879-2885 | 7 | |
| α-helix | 2890-2903 | 14 | |
| α-helix | 2918-2922 | 5 | |
| α-helix | 2925-2942 | 18 | |
| α-helix | 2943-2946 | 4 | |
| α-helix | 2955-2959 | 5 | |
| α-helix | 2961-2964 | 4 | |
| α-helix | 2984-2991 | 8 | |
| α-helix | 2998-3008 | 11 | |
| α-helix | 3015-3032 | 18 | |
| α-helix | 3042-3068 | 27 | |
| α-helix | 3088-3093 | 6 | |
| α-helix | 3099-3102 | 4 | |
| α-helix | 3112-3114 | 3 | |
| α-helix | 3116-3123 | 8 | |
| α-helix | 3134-3145 | 12 | |
| α-helix | 3150-3154 | 5 | |
| α-helix | 3203-3206 | 4 | |
| α-helix | 3212-3217 | 6 | |
| α-helix | 3233-3240 | 8 | |
| α-helix | 3254-3268 | 15 | |
| α-helix | 3288-3307 | 20 | |
| α-helix | 3317-3328 | 12 | |
| α-helix | 3337-3357 | 21 | |
| α-helix | 3365-3387 | 23 | |
| α-helix | 3393-3396 | 4 | |
| α-helix | 3405-3411 | 7 | |
| α-helix | 3413-3416 | 4 | |
| α-helix | 3428-3440 | 13 | |
| β-strand | 3443 | 1 | 1 |
| α-helix | 3448-3462 | 15 | |
| α-helix | 3474-3483 | 10 | |
| α-helix | 3486-3510 | 25 | |
| α-helix | 3518-3543 | 26 | |
| β-strand | 3546 | 1 | 1 |
| α-helix | 3548-3553 | 6 | |
| α-helix | 3581-3585 | 5 | |
| α-helix | 3604-3616 | 13 | |
| α-helix | 3620-3622 | 3 | |
| α-helix | 3624-3639 | 16 | |
| α-helix | 3653-3673 | 21 | |
| α-helix | 3691-3694 | 4 | |
| α-helix | 3707-3711 | 5 | |
| α-helix | 3720-3726 | 7 | |
| α-helix | 3738-3754 | 17 | |
| α-helix | 3757-3779 | 23 | |
| α-helix | 3793-3804 | 12 | |
| α-helix | 3806-3821 | 16 | |
| α-helix | 3828-3830 | 3 | |
| α-helix | 3831-3838 | 8 | |
| α-helix | 3841-3844 | 4 | |
| α-helix | 3855-3857 | 3 | |
| α-helix | 3858-3877 | 20 | |
| α-helix | 3885-3897 | 13 | |
| α-helix | 3914-3924 | 11 | |
| α-helix | 3928-3935 | 8 | |
| α-helix | 3949-3963 | 15 | |
| α-helix | 3965-3980 | 16 | |
| α-helix | 3993-3996 | 4 | |
| α-helix | 4000-4006 | 7 | |
| α-helix | 4010-4040 | 31 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Midasin,Midasin,Midasin | A | protein | 1676 | Saccharomyces cerevisiae | Q12019 |
>6HYD_1 Midasin,Midasin,Midasin (chains A) PIEESLAAVIPISHLGEVGKWANNVLNCTEYSEKKIAERLYVFITFLTDMGVLEKINNLY KPANLKFQKALGLHDKQLTEETVSLTLNEYVLPTVSKYSDKIKSPESLYLLSSLRLLLNS LNALKLINEKSTHGKIDELTYIELSAAAFNGRHLKNIPRIPIFCILYNILTVMSENLKTE SLFCGSNQYQYYWDLLVIVIAALETAVTKDEARLRVYKELIDSWIASVKSKSDIEITPFL NINLEFTDVLQLSRGHSITLLWDIFRKNYPTTSNSWLAFEKLINLSEKFDKVRLLQFSES YNSIKDLMDVFRLLNDDVLNNKLSEFNLLLSKLEDGINELELISNKFLNKRKHYFADEFD NLIRYTFSVDTAELIKELAPASSLATQKLTKLITNKYNYPPIFDVLWTEKNAKLTSFTST IFSSQFLEDVVRKSNNLKSFSGNQIKQSISDAELLLSSTIKCSPNLLKSQMEYYKNMLLS WLRKVIDIHVGGDCLKLTLKELCSLIEEKTASETRVTFAEYIFPALDLAESSKSLEELGE AWITFGTGLLLLFVPDSPYDPAIHDYVLYDLFLKTKTFSQNLMKSWRNVRKVISGDEEIF TEKLINTISDDDAPQSPRVYRTGMSIDSLFDEWMAFLSSTMSSRQIKELVSSYKCNSDQS DRRLEMLQQNSAHFLNRLESGYSKFADLNDILAGYIYSINFGFDLLKLQKSKDRASFQIS PLWSMDPINISCAENVLSAYHELSRFFKKGDMEDTSIEKVLMYFLTLFKFHKRDTNLLEI FEAALYTLYSRWSVRRFRQEQEENEKSNMFKFNDNSDDYEADFRKLFPDYEDTALVTNEK DISSPENLDDIYFKLADTYISVFDKDHDANFSSELKSGAIITTILSEDLKNTRIEELKSG SLSAVINTLDAETQSFKNTEVFGNIDFYHDFSIPEFQKAGDIIETVLKSVLKLLKQWPEH ATLKELYRVSQEFLNYPIKTPLARQLQKIEQIYTYLAEWEKYASSEVSLNNTVKLITDLI VSWRKLELRTWKGLFNSEDAKTRKSIGKWWFYLYESIVISNFVSEKKETAPNATLLVSSL NLFFSKSTLGEFNARLDLVKAFYKHIQLIGLRSSKIAGLLHNTIKFYYQFKPLIDERITN GKKSLEKEIDDIILLASWKDVNVDALKQSSRKSHNNLYKIVRKYRDLLNGDAKTIIEAGL LYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXRNIDTVASNMDSYLEKISSQEFPNFAD LASDFYAEAERLRKETPNVYTKENKKRLAYLKTQKSKLLGDALKELRRIGLKVNFREDIQ KVQSSTTTILANIAPFNNEYLNSSDAFFFKILDLLPKLRSAASNPSDDIPVAAIERGMAL AQSLMFSLITVRHPLSEFTNDYCKINGMMLDLEHFTCLKGDIVHSSLKANVDNVRLFEKW LPSLLDYAAQTLSVISKYSATSEQQKILLDAKSTLSSFFVHFNSSRIFDSSFIESYSRFE LFINELLKKLENAKETGNAFVFDIIIEWIKANKGGPIKKEQKRGPSVEDVEQAFRRTFTS IILSFQKVIGDGIESISETDDNWLSASFKKVMVNVKLLRSSVVSKNIETALSLLKDFDFT TTESIYVKSVISFTLPVITRYYNAMTVVLERSRIYYTNTSRGMYILSTILHSLAKN
The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1. Sosnowski, P., Urnavicius, L., Boland, A. et al. Elife (2018) 7. DOI 10.7554/eLife.39163 · PubMed
Other PDB entries of the same protein (UniProt Q12019), best resolution first:
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