| Link type | Probability | Chain A piercings | Chain D piercings | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
| view details |
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Hopf.2 | 56% | +87D -155D -160D | -95A +119A -132A | ||||||||
Chain A Sequence |
MSLPDGFYIRRMEEGDLEQVTETLKVLTTVGTITPESFCKLIKYWNEATVWND---KKIMQYNPMVIVDKRTETVAATGNIIIERKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEMQIRK |
Chain A Sequence |
GSMSLPDGFYIRRMEEGDLEQVTETLKVLTTVGTITPESFCKLIKYWNEATVWNDNEDKKIMQYNPMVIVDKRTETVAATGNIIIERKIIHELGLCGHIEDIAVNSKYQGQGLGKLLIDQLVTIGFDYGCYKIILDCDEKNVKFYEKCGFSNAGVEMQIRK |
| sequence length | 159,161 |
| structure length | 156,161 |
| publication title |
The crystal structures of Apo and complexed Saccharomyces cerevisiae GNA1 shed light on the catalytic mechanism of an amino-sugar N-acetyltransferase.
pubmed doi rcsb |
| molecule tags | Transferase |
| molecule keywords | GLUCOSAMINE-PHOSPHATE N-ACETYLTRANSFERASE |
| source organism | Saccharomyces cerevisiae |
| missing residues | A: 53-57 |
| ec nomenclature |
ec 2.3.1.4: Glucosamine-phosphate N-acetyltransferase. ec 2.3.1.4: Glucosamine-phosphate N-acetyltransferase. |
| pdb deposition date | 2001-02-01 |
| LinkProt deposition date | 2016-10-21 |
| chain | Pfam Accession Code | Pfam Family Identifier | Pfam Description |
|---|---|---|---|
| AD | PF00583 | Acetyltransf_1 | Acetyltransferase (GNAT) family |
| AD | PF00583 | Acetyltransf_1 | Acetyltransferase (GNAT) family |
Image from the rcsb pdb (www.rcsb.org)cath code
| Class | Architecture | Topology | Homology | Domain |
|---|---|---|---|---|---|
| Alpha Beta | 3-Layer(aba) Sandwich | Aminopeptidase | Aminopeptidase | ||
| Alpha Beta | 3-Layer(aba) Sandwich | Aminopeptidase | Aminopeptidase |
#chains in the LinkProt database with same CATH superfamily 1I21 AB; 1I21 BMXY; 1I21 BMN; 1I21 BMY; 1I21 BM; 1I21 AMN; 1I21 BXY; 1I1D AD; 1I21 BY; 1I21 BNY; 1I1D BC; 1I21 ABY; 1I21 ABXY; 1I21 ABN; 1I21 ABM; 1I21 XY; 1I21 BNXY; 1I21 AM; 1I21 ABMY; 1I21 ABNY; 1I21 BMNY; 1I21 BN; 1I21 ABMN; 1I21 MN; #chains in the LinkProt database with same CATH topology 1I21 AB; 1I21 BMXY; 1I21 BMN; 1I21 BMY; 1I21 BM; 1I21 AMN; 1I21 BXY; 1I1D AD; 1I21 BY; 1I21 BNY; 1I1D BC; 1I21 ABY; 1I21 ABXY; 1I21 ABN; 1I21 ABM; 1I21 XY; 1I21 BNXY; 1I21 AM; 1I21 ABMY; 1I21 ABNY; 1I21 BMNY; 1I21 BN; 1I21 ABMN; 1I21 MN; #chains in the LinkProt database with same CATH homology 1I21 AB; 1I21 BMXY; 1I21 BMN; 1I21 BMY; 1I21 BM; 1I21 AMN; 1I21 BXY; 1I1D AD; 1I21 BY; 1I21 BNY; 1I1D BC; 1I21 ABY; 1I21 ABXY; 1I21 ABN; 1I21 ABM; 1I21 XY; 1I21 BNXY; 1I21 AM; 1I21 ABMY; 1I21 ABNY; 1I21 BMNY; 1I21 BN; 1I21 ABMN; 1I21 MN;
#similar chains in the LinkProt database (?% sequence similarity) ...loading similar chains, please wait... #similar chains, but unlinked ...loading similar chains, please wait... #similar chains in the pdb database (?% sequence similarity) ...loading similar chains, please wait...
