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 |
251
|
sequence length |
797
|
structure length |
795
|
Chain Sequence |
DAEARELALAGMGASRLRKEDARFIQGKGNYVDDIKMPGMLHMDIVRAPIAHGRIKKIHKDAALAMPGVHAVLTAEDLKPLKLHWMPTLAGDVAAVLADEKVHFQMQEVAIVIADDRYIAADAVEAVKVEYDELPVVIDPIDALKPDAPVLREDLAGKTSGAHGPREHHNHIFTWGAGDKAATDAVFANAPVTVSQHMYYPRVHPCPLETCGCVASFDPIKGDLTTYITSQAPHVVRTVVSMLSGIPESKVRIVSPDIGGGFGNKVGIYPGYVCAIVASIVLGRPVKWVEDRVENISTTAFARDYHMDGELAATPDGKILGLRVNVVADHGAFDACADPTKFPAGLFHICSGSYDIPRAHCSVKGVYTNKAPGGVAYSFRVTEAVYLIERMVDVLAQKLNMDKAEIRAKNFIRKEQFPYTTQFGFEYDSGDYHTALKKVLDAVDYPALRAEQAARRADPNSPTLMGIGLVTFTEVVGAGPSKMCDILGVGMFDSCEIRIHPTGSAIARMGTITQGQGHQTTYAQIIATELGIPSEVIQVEEGDTSTAPYGLGTYGSRSTPVAGAAIALAARKIHAKARKIAAHMLEVNENDLDWEVDRFKVKGDDSKFKTMADIAWQAYHQPPAGLEPGLEAVHYYDPPNFTYPFGIYLCVVDIDRATGETKVRRFYALDDCGTRINPMIIEGQIHGGLTEGYAVAMGQQMPFDAQGNLLGNTLMDYFLPTAVETPHWETDHTVTPSPHHPIGAKGVAESPHVGSIPTFTAAVVDAFAHVGVTHLDMPHTSYRVWKSLKEHNLAL
|
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 effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.
pubmed doi rcsb |
| molecule keywords |
CUTS, IRON-SULFUR PROTEIN OF CARBON MONOXIDE DEHYDROGENASE
|
| molecule tags |
Hydrolase
|
| total genus |
251
|
| structure length |
795
|
| sequence length |
797
|
| chains with identical sequence |
E
|
| ec nomenclature |
ec
1.2.5.3: Aerobic carbon monoxide dehydrogenase. |
| pdb deposition date | 2000-07-26 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| B | PF01315 | Ald_Xan_dh_C | Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain |
| B | PF02738 | Ald_Xan_dh_C2 | Molybdopterin-binding domain of aldehyde dehydrogenase |
Image from the rcsb pdb (www.rcsb.org)
cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Alpha Beta | 2-Layer Sandwich | Aldehyde Oxidoreductase; domain 4 | Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain | ||
| Alpha Beta | 2-Layer Sandwich | Aldehyde Oxidoreductase; domain 4 | Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain | ||
| Alpha Beta | 2-Layer Sandwich | Aldehyde Oxidoreductase; domain 4 | Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain | ||
| Alpha Beta | 2-Layer Sandwich | Aldehyde Oxidoreductase; domain 4 | Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain | ||
| Alpha Beta | Alpha-Beta Complex | Aldehyde Oxidoreductase; domain 3 | Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead |
#chains in the Genus database with same CATH superfamily 3AMZ A; 4US9 A; 1VDV A; 3AN1 A; 1N63 B; 2W54 B; 3FC4 A; 4C7Y A; 3L4P A; 1JRO B; 1SIJ A; 3NRZ C; 3NVV C; 3NVY C; 3NVZ C; 3AM9 A; 3ETR C; 1WYG A; 1JRP B; 3SR6 C; 4US8 A; 1FFV B; 1SB3 A; 3HRD B; 1N62 B; 3EUB 4; 2W55 B; 2E3T A; 2W3R B; 4ZOH A; 4USA A; 4C80 A; 1DGJ A; 1FO4 A; 1FIQ C; 3FAH A; 1N61 B; 4C7Z A; 1N5W B; 1V97 A; 3HRD A; 1N5X A; 1ZXI B; 2W3S B; 3B9J C; 3NS1 C; 1RM6 A; 1VLB A; 3NVW C; 1N60 B; 1FFU B; #chains in the Genus database with same CATH topology 1Q82 J; 1Q81 J; 3AN1 A; 3C2E A; 1N63 B; 2W54 B; 3FC4 A; 1BRW A; 2ZJP J; 2J0F A; 5DM6 J; 2Q5W E; 4EAD A; 1SIJ A; 4YEK A; 3OW2 H; 3CXC H; 4IOC J; 2OTL H; 1VQ9 H; 3WNZ A; 3NVY C; 2ZJR J; 1VQ8 H; 1QVF H; 5AN9 F; 4X46 A; 1JRP B; 1QPQ A; 3CF5 J; 3CCS H; 1YJ9 H; 1VQO H; 4I9A A; 4AP8 A; 2PA2 A; 1WKI A; 5EY3 A; 2W55 B; 2E3T A; 1YTE A; 2TPT A; 2OMD A; 4LHM A; 3TQV A; 4ZOH A; 1JJ2 H; 4C80 A; 1VQ7 H; 1DGJ A; 1M1K J; 1YTD A; 2I1O A; 1K73 J; 1AZY A; 3PAJ A; 1K8A J; 4C7Z A; 1N5W B; 3HRD A; 1N5X A; 1RM6 A; 1VLB A; 3NVW C; 3C2V A; 3CCJ H; 1W2B H; 3CCL H; 3PIO J; 3CPW H; 5GAE N; 5HUO A; 5H1S O; 3L4P A; 3CCE H; 1KC8 J; 1JRO B; 4KWV A; 1VQ5 H; 5MLC O; 3WO0 A; 1O4U A; 3NVZ C; 3CCU H; 1N8R J; 3I56 H; 3SR6 C; 4US8 A; 1YHQ H; 1SB3 A; 3HRD B; 1FM0 E; 3EUB 4; 2QEX H; 3VMM A; 3J7Z M; 1VQK H; 1NVJ A; 5AYZ A; 1YTK A; 3FAH A; 3CC2 H; 1V97 A; 2WP4 A; 1ZXI B; 2W3S B; 2WK6 A; 4WCE J; 2QIE A; 3L0G A; 1YIJ H; 3G71 H; 4YYY A; 4XR5 A; 3CME H; 2JBM A; 3AMZ A; 4US9 A; 1VDV A; 4GA4 A; 1T3Q B; 3CC4 H; 5JVH J; 1YJN H; 4C7Y A; 1QAP A; 3C2R A; 5HUP A; 2ZJQ J; 1Y69 K; 1OTP A; 3CCM H; 3CCV H; 4WFB J; 1NJI J; 3CC7 H; 1QVG H; 3ETR C; 2WK5 A; 4U67 J; 1FFV B; 4WFA J; 3G6E H; 1VQL H; 4WFN J; 5GAH N; 4IO9 J; 4USA A; 2B7Q A; 5MPO C; 1FO4 A; 5JVG J; 1Q86 J; 5DM7 J; 1FIQ C; 2B7N A; 3C2O A; 2QA4 H; 5GAG N; 3BII E; 3I55 H; 3RPF A; 1QPO A; 1QPR A; 1N60 B; 1FFU B; 1VQN H; 3CCQ H; 3CD6 H; 1YIT H; 5HUL A; 3G4S H; 3C2F A; 4KWW A; 2DSJ A; 1VQP H; 1Q7Y J; 3CMA H; 3NRZ C; 3NVV C; 3PIP J; 1YI2 H; 3DLL J; 2B7P A; 3AM9 A; 1WYG A; 3H5Q A; 5AYY A; 5HL7 J; 1QPN A; 1VQ6 H; 1N62 B; 1NVI E; 3WO1 A; 5GAD N; 1VQM H; 3GNN A; 1KQS H; 1YJW H; 1X1O A; 2W3R B; 3CCR H; 1S72 H; 4WF9 J; 2I14 A; 1K9M J; 5EP8 A; 2OTJ H; 1N61 B; 4IOA J; 4GA5 A; 1VQ4 H; 4EAF A; 4UY8 M; 4GA6 A; 3B9J C; 3NS1 C; 1UOU A; 1M90 J; 1KD1 J; 5AYX A; 1FMA E; #chains in the Genus database with same CATH homology 3AMZ A; 4US9 A; 1VDV A; 3AN1 A; 1N63 B; 2W54 B; 3FC4 A; 4C7Y A; 3L4P A; 1JRO B; 1SIJ A; 3NRZ C; 3NVV C; 3NVY C; 3NVZ C; 3AM9 A; 3ETR C; 1WYG A; 1JRP B; 3SR6 C; 4US8 A; 1FFV B; 1SB3 A; 3HRD B; 1N62 B; 3EUB 4; 2W55 B; 2E3T A; 2W3R B; 4ZOH A; 4USA A; 4C80 A; 1DGJ A; 1FO4 A; 1FIQ C; 3FAH A; 1N61 B; 4C7Z A; 1N5W B; 1V97 A; 3HRD A; 1N5X A; 1ZXI B; 2W3S B; 3B9J C; 3NS1 C; 1RM6 A; 1VLB A; 3NVW C; 1N60 B; 1FFU B;
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