The genus trace: a function that shows values of genus (vertical axis) for subchains spanned between the first residue, and all other residues (shown on horizontal axis). The number of the latter residue and the genus of a given subchain are shown interactively.
Total Genus |
168
|
sequence length |
573
|
structure length |
523
|
Chain Sequence |
HIDLYQQIKWNGWGDTRKFLHQLKPSGTIAMTTPEVSSVPLPSLRGFIKKELTFVLDETPALQIENIHVDPPKQYPEFVRELKAFFLPDQLKDDKLARITHTFGKSLRDLIRVRIGQVKNAPDLIVLPHSHEEVERLVQLAHKYNVVIIPMGGGSNIVGAIEPVSNERFTVSIDMRRMNKVLWVDRREMTACIQVGIMGPELEKQLHKQGVSLGHDPDSFEFSTLGGWLATCSSGHQSDKYGDIEDMAVSFRTVTPTGTLELRGINYKHIILGSEGTLGIITEAVMKVHAVPQAVEYYGFLFPTFAHAVSALQQIRSSEVIPTMIRVYDPEETQLSFAWKPTSAMVKKYLHYIRSFDFKNVCLSIIGFEGPKKVVDFHRTSVFDILSKNAAFGLGSAPGKTWAEKRYDLPYIRDFLLDHNMWVDVAETTVSYANLQTLWKDAKQTFVKHFKDQGIPAWICAHISHTYTNGVCLYFIFASKQNYIEAKKLMTDIIFKYGGSRGWINVYRSLKETIDPKDICNPR
|
The genus matrix. At position (x,y) a genus value for a subchain spanned between x’th and y’th residue is shown. Values of the genus are represented by color, according to the scale given on the right.
After clicking on a point (x,y) in the genus matrix above, a subchain from x to y is shown in color.
publication title |
The Crucial Step in Ether Phospholipid Biosynthesis: Structural Basis of a Noncanonical Reaction Associated with a Peroxisomal Disorder.
pubmed doi rcsb |
molecule tags |
Transferase
|
source organism |
Dictyostelium discoideum
|
molecule keywords |
ALKYLDIHYDROXYACETONEPHOSPHATE SYNTHASE
|
total genus |
168
|
structure length |
523
|
sequence length |
573
|
chains with identical sequence |
B, C, D
|
ec nomenclature |
ec
2.5.1.26: Alkylglycerone-phosphate synthase. |
pdb deposition date | 2007-03-07 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF01565 | FAD_binding_4 | FAD binding domain |
A | PF02913 | FAD-oxidase_C | FAD linked oxidases, C-terminal domain |
cath code
| Class | Architecture | Topology | Homology | Domain |
---|---|---|---|---|---|
Alpha Beta | 2-Layer Sandwich | Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 | Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 | ||
Alpha Beta | 3-Layer(aba) Sandwich | Vanillyl-alcohol Oxidase; Chain A, domain 3 | Vanillyl-alcohol Oxidase; Chain A, domain 3 |
#chains in the Genus database with same CATH superfamily 2Y4G A; 2Y3S A; 3HSU A; 2UUU A; 5L6G A; 5K8E A; 3RJA A; 2Y08 A; 3PQB A; 2WDW A; 3POP A; 5AWV A; 2IPI A; 5I1V A; 2UUV A; 2Y3R A; 3RJ8 A; 5I1W A; 5L6F A; #chains in the Genus database with same CATH topology 3NVW B; 2EXR A; 4EC3 A; 2MBR A; 1FFV C; 2GQT A; 2Y4G A; 3ETR B; 3EUB 3; 1W1Q A; 1ZR6 A; 2AXR A; 1AHV A; 2OAI A; 3NVZ B; 1UXY A; 2VFT A; 4XLO A; 4MLA A; 2UUU A; 1N5W C; 5AE1 A; 2W55 A; 2VFR A; 4PZF A; 3FW7 A; 5D79 A; 3AM9 A; 3RJA A; 5HMR A; 5AE3 A; 3PQB A; 3POP A; 1AHU A; 2IPI A; 3AMZ A; 2P3H A; 2Y3R A; 2I0K A; 3W8X A; 4ML8 A; 1N63 C; 2Q4W A; 1N60 C; 3W8W A; 5G5H B; 2VFS A; 5G5G B; 1DIQ A; 3S1F A; 5FXP A; 3D2J A; 1V97 A; 2BVH A; 1FFU C; 4PVE A; 1FIQ B; 3DQ0 A; 5FXD A; 2R2Z A; 1MBB A; 2QPM A; 3NVY B; 2PLI A; 4PVH A; 3C0P A; 1F0X A; 4BC7 A; 1DII A; 4JAY A; 1E8H A; 1I19 A; 5L6G A; 2RK5 A; 2GQU A; 5K8E A; 1W1J A; 4UD8 A; 5FXE A; 5FXF A; 1RM6 B; 1QLU A; 3NS1 B; 1JRP A; 3NVV B; 2O3G A; 4OAL A; 5I1V A; 1AHZ A; 3D2D A; 4BCA A; 4HG0 A; 4JB1 A; 1W1S A; 4PWC A; 1DZN A; 3RJ8 A; 3AN1 A; 2QKN A; 5L6F A; 5ADZ A; 3FWA A; 3FW9 A; 1W1O A; 1W1M A; 2W3S A; 3TSH A; 5HQX A; 1W1K A; 1ZXI C; 3TX1 A; 2YVS A; 4BBY A; 4O95 A; 2BVF A; 2Y3S A; 1MBT A; 1W1R A; 1E0Y A; 2VFU A; 1WVE A; 1WVF A; 2R8D A; 3D2H A; 3LLB A; 1N5X A; 1VDV A; 3VTE A; 3BW7 A; 1QLT A; 1JRO A; 2UUV A; 2PLS A; 1E8F A; 3PM9 A; 1N61 C; 2VFV A; 3I99 A; 3S1E A; 5I1W A; 1HSK A; 1WYG A; 2W3R A; 3FW8 A; 2P13 A; 2BVG A; 3GSY A; 3JS8 A; 4PVJ A; 1W1L A; 2P4P A; 2W54 A; 3LAE A; 5HHZ A; 3W8Z A; 4PWB A; 1SB3 B; 2Q85 A; 3DED A; 3NRZ B; 3HSU A; 3HRD C; 2VAO A; 1E8G A; 3TSJ A; 3B9J B; 1FO4 A; 3KJM A; 3S1D A; 2Y08 A; 2WDW A; 4PVK A; 5AWV A; 4BC9 A; 3SR6 B; 2E3T A; 1VAO A; 4ZOH B; 1T3Q C; 4PYT A; 3S1C A; 4DNS A; 5AE2 A; 1N62 C; 2NQW A; #chains in the Genus database with same CATH homology 3NVW B; 2EXR A; 4EC3 A; 2MBR A; 1FFV C; 2GQT A; 2Y4G A; 3ETR B; 3EUB 3; 1W1Q A; 1ZR6 A; 2AXR A; 1AHV A; 2OAI A; 3NVZ B; 1UXY A; 2VFT A; 4XLO A; 4MLA A; 2UUU A; 1N5W C; 5AE1 A; 2W55 A; 2VFR A; 4PZF A; 3FW7 A; 5D79 A; 3AM9 A; 3RJA A; 5HMR A; 5AE3 A; 3PQB A; 3POP A; 1AHU A; 2IPI A; 3AMZ A; 2P3H A; 2Y3R A; 2I0K A; 3W8X A; 4ML8 A; 1N63 C; 2Q4W A; 1N60 C; 3W8W A; 5G5H B; 2VFS A; 5G5G B; 1DIQ A; 3S1F A; 5FXP A; 3D2J A; 1V97 A; 2BVH A; 1FFU C; 4PVE A; 1FIQ B; 3DQ0 A; 5FXD A; 2R2Z A; 1MBB A; 2QPM A; 3NVY B; 2PLI A; 4PVH A; 3C0P A; 1F0X A; 4BC7 A; 1DII A; 4JAY A; 1E8H A; 1I19 A; 5L6G A; 2RK5 A; 2GQU A; 5K8E A; 1W1J A; 4UD8 A; 5FXE A; 5FXF A; 1RM6 B; 1QLU A; 3NS1 B; 1JRP A; 3NVV B; 2O3G A; 4OAL A; 5I1V A; 1AHZ A; 3D2D A; 4BCA A; 4HG0 A; 4JB1 A; 1W1S A; 4PWC A; 1DZN A; 3RJ8 A; 3AN1 A; 2QKN A; 5L6F A; 5ADZ A; 3FWA A; 3FW9 A; 1W1O A; 1W1M A; 2W3S A; 3TSH A; 5HQX A; 1W1K A; 1ZXI C; 3TX1 A; 2YVS A; 4BBY A; 4O95 A; 2BVF A; 2Y3S A; 1MBT A; 1W1R A; 1E0Y A; 2VFU A; 1WVE A; 1WVF A; 2R8D A; 3D2H A; 3LLB A; 1N5X A; 1VDV A; 3VTE A; 3BW7 A; 1QLT A; 1JRO A; 2UUV A; 2PLS A; 1E8F A; 3PM9 A; 1N61 C; 2VFV A; 3I99 A; 3S1E A; 5I1W A; 1HSK A; 1WYG A; 2W3R A; 3FW8 A; 2P13 A; 2BVG A; 3GSY A; 3JS8 A; 4PVJ A; 1W1L A; 2P4P A; 2W54 A; 3LAE A; 5HHZ A; 3W8Z A; 4PWB A; 1SB3 B; 2Q85 A; 3DED A; 3NRZ B; 3HSU A; 3HRD C; 2VAO A; 1E8G A; 3TSJ A; 3B9J B; 1FO4 A; 3KJM A; 3S1D A; 2Y08 A; 2WDW A; 4PVK A; 5AWV A; 4BC9 A; 3SR6 B; 2E3T A; 1VAO A; 4ZOH B; 1T3Q C; 4PYT A; 3S1C A; 4DNS A; 5AE2 A; 1N62 C; 2NQW A;
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