Knot core range | Knot core length | Knot tails range | Slipknot tails range | Slipknot loops range | N-end length | C-end length | Type | |||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
view details | +31 | 24-253 | 230 | 254-258 | 1-1 | 2-23 | 1 | 4 | slipknot |
Chain Sequence |
HWGYGKHNGPEHWHKDFPICKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPCLESVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
|
Knot core range | Knot core length | Knot tails range | Slipknot tails range | Slipknot loops range | N-end length | C-end length | Type | ||||
---|---|---|---|---|---|---|---|---|---|---|---|
+ 31 | 23-255 | 233 | 1-22, 256-258 | 22 | 3 | knot |
Fingerprint | Knot forming loop | Loop type | ||||
---|---|---|---|---|---|---|
|
K +31 | His4 ... His94 <-> Bridging ionZn301 <-> His96 ... Chain closureLys261 <-> His4 |
probabilistic | |||
|
K +31 | His4 ... His96 <-> Bridging ionZn301 <-> His119 ... Chain closureLys261 <-> His4 |
probabilistic | |||
|
K +31 | His4 ... His94 <-> Bridging ionZn301 <-> His119 ... Chain closureLys261 <-> His4 |
probabilistic |
Chain Sequence |
HWGYGKHNGPEHWHKDFPICKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPCLESVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
|
Knotoid cutoff: 0.5
Knotoid matrix content: 1
Knot core range | Knot core length | Knot tails range | Slipknot tails range | Slipknot loops range | N-end length | C-end length | Type | |||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
view details | 3.1 | 25-256 | 232 | 1-24, 257-257 | 24 | 1 | knot | |||||
view details | 2.1 | 24-251 | 228 | 1-23 | 257-257 | 252-256 | 23 | 1 | slipknot |
sequence length |
257
|
structure length |
257
|
publication title |
Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond.
pubmed doi rcsb |
molecule tags |
Lyase
|
molecule keywords |
Carbonic anhydrase 2
|
source organism |
Homo sapiens
|
total genus |
Genus: 74
|
ec nomenclature |
ec
4.2.1.1: Carbonate dehydratase. |
pdb deposition date | 2012-09-27 |
KnotProt deposition date | 2018-10-03 |
chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
---|---|---|---|
A | PF00194 | Carb_anhydrase | Eukaryotic-type carbonic anhydrase |
#similar chains in the KnotProt database (?% sequence similarity) ...loading similar chains, please wait... #similar chains, but unknotted ...loading similar chains, please wait... #similar chains in the pdb database (?% sequence similarity) ...loading similar chains, please wait...