GL1X · GenesisL1 explorer

UniProt P25515

V-type proton ATPase subunit c (P25515)

V-type proton ATPase subunit c (UniProt P25515): 29 experimental structures and 1 predicted model on GenesisL1, 3 ligands bound, 38 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P25515
Protein
V-type proton ATPase subunit c
Experimental structures
29
Predicted models
1
Ligands
3
Pockets
38 · 4 records with a druggable one

Structures

30 records of P25515 in the MolNFT archive: 29 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
3J9TYeast V-ATPase state 1electron microscopyY, R, U, V, T, W, S, X, Z, a——
3J9UYeast V-ATPase state 2electron microscopyU, X, a, R, Z, S, Y, T, V, W——
3J9VYeast V-ATPase state 3electron microscopyR, U, X, Y, W, Z, V, a, S, T——
5TJ5Atomic model for the membrane-embedded motor of a eukaryotic V-ATPaseelectron microscopyE, F, G, H, I, J, M, N——
5VOXYeast V-ATPase in complex with legionella pneumophila effector sidk (rotational state 1)electron microscopyT, U, V, W, X, Y, Z, a——
5VOYYeast V-ATPase in complex with legionella pneumophila effector sidk (rotational state 2)electron microscopyT, U, V, W, X, Y, Z, a——
5VOZYeast V-ATPase in complex with legionella pneumophila effector sidk (rotational state 3)electron microscopyT, U, V, W, X, Y, Z, a——
6C6LYeast vacuolar ATPase vo in lipid nanodiscelectron microscopyE, F, G, H, I, J, K, L——
6M0R2.7A yeast vo STATE3electron microscopyE, F, G, H, I, J, K, LPEE—
6M0S3.6A Yeast Vo state3 primeelectron microscopyE, F, G, H, I, J, K, L—14 (best 0.81)
6M0S3.6A yeast vo STATE3 primeelectron microscopyE, F, G, H, I, J, K, L——
6O7TSaccharomyces cerevisiae V-ATPase Vph1-VOelectron microscopyg, h, i, j, k, l, m, n——
6O7TSaccharomyces cerevisiae V-ATPase VPH1-voelectron microscopyg, h, i, j, k, l, m, n——
6O7USaccharomyces cerevisiae V-ATPase STV1-voelectron microscopyg, h, i, j, k, l, m, n——
6O7VSaccharomyces cerevisiae V-ATPase STV1-V1VO state 1electron microscopyg, h, i, j, k, l, m, n——
6O7WSaccharomyces cerevisiae V-ATPase Stv1-V1VO State 2electron microscopyg, h, i, j, k, l, m, n——
6O7WSaccharomyces cerevisiae V-ATPase STV1-V1VO state 2electron microscopyg, h, i, j, k, l, m, n——
6O7XSaccharomyces cerevisiae V-ATPase Stv1-V1VO State 3electron microscopyg, h, i, j, k, l, m, n—2 (best 0.84)
6O7XSaccharomyces cerevisiae V-ATPase STV1-V1VO state 3electron microscopyg, h, i, j, k, l, m, n——
6PE4Yeast Vo motor in complex with 1 VopQ moleculeelectron microscopyI, J, K, L, M, N, O, P—13 (best 0.82)
6PE4Yeast vo motor in complex with 1 vopq moleculeelectron microscopyI, J, K, L, M, N, O, P——
6PE5Yeast vo motor in complex with 2 vopq moleculeselectron microscopyI, J, K, L, M, N, O, P——
7FDACryoem structure of reconstituted V-ATPase, STATE1electron microscopyV, W, X, Y, Z, a, b, c——
7FDBCryoem structures of reconstituted V-ATPASE,STATE2electron microscopyV, W, X, Y, Z, a, b, c——
7FDCCryoem structures of reconstituted V-ATPase, STATE3electron microscopyV, W, X, Y, Z, a, b, c——
7TAOCryo-EM structure of bafilomycin A1 bound to yeast vo V-ATPaseelectron microscopyE, F, G, H, I, J, K, LWEV—
7TAPCryo-EM structure of archazolid a bound to yeast vo V-ATPaseelectron microscopyE, F, G, H, I, J, K, LKJL—
7TMRV-ATPase from saccharomyces cerevisiae, state 1electron microscopyg, h, i, j, k, l, m, n——
8EATYeast VO missing subunits a, e, and f in complex with Vma12-22pelectron microscopyg, h, i, j, k, l, m, n—9 (best 0.76)
P25515AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit C (P25515)predictedA——

Ligands

  • KJL · Archazolid A · in 1 record
  • PEE · 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine · in 1 record
  • WEV · (5R)-2,4-dideoxy-1-C-{(2S,3R,4S)-3-hydroxy-4-[(2R,3S, 4E,6E,9R,10S,11R,12E,14Z)-10-hydroxy-3,15-dimethoxy-7, 9,11,13-tetramethyl-16-oxo-1-oxacyclohexadeca-4,6,12, 14-tetraen-2-yl]pentan-2-yl}-4-methyl-5-propan-2-yl-alpha-D-threo-pentopyranose · in 1 record

Experiment against prediction

Elsewhere

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.