6XB3
Structure of AcNPV poxin in post-reactive state with Gp[2'-5']Ap[3']
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004518 | molecular_function | nuclease activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| B | 0004518 | molecular_function | nuclease activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| C | 0004518 | molecular_function | nuclease activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| D | 0004518 | molecular_function | nuclease activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| E | 0004518 | molecular_function | nuclease activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| F | 0004518 | molecular_function | nuclease activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| G | 0004518 | molecular_function | nuclease activity |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| H | 0004518 | molecular_function | nuclease activity |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| I | 0004518 | molecular_function | nuclease activity |
| I | 0016787 | molecular_function | hydrolase activity |
| I | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| J | 0004518 | molecular_function | nuclease activity |
| J | 0016787 | molecular_function | hydrolase activity |
| J | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| K | 0004518 | molecular_function | nuclease activity |
| K | 0016787 | molecular_function | hydrolase activity |
| K | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| L | 0004518 | molecular_function | nuclease activity |
| L | 0016787 | molecular_function | hydrolase activity |
| L | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| M | 0004518 | molecular_function | nuclease activity |
| M | 0016787 | molecular_function | hydrolase activity |
| M | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| N | 0004518 | molecular_function | nuclease activity |
| N | 0016787 | molecular_function | hydrolase activity |
| N | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| O | 0004518 | molecular_function | nuclease activity |
| O | 0016787 | molecular_function | hydrolase activity |
| O | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
| P | 0004518 | molecular_function | nuclease activity |
| P | 0016787 | molecular_function | hydrolase activity |
| P | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue 9BG A 301 |
| Chain | Residue |
| A | SER172 |
| A | ARG226 |
| A | HOH437 |
| A | HOH450 |
| A | HOH464 |
| A | HOH488 |
| A | HOH493 |
| A | HOH515 |
| B | SER43 |
| B | TYR45 |
| B | HIS46 |
| A | VAL173 |
| B | GLN47 |
| B | PHE48 |
| B | ARG93 |
| B | ILE146 |
| B | ARG147 |
| B | SER153 |
| B | HIS155 |
| B | HOH447 |
| B | HOH491 |
| A | TYR181 |
| A | ILE184 |
| A | LYS185 |
| A | ALA188 |
| A | LEU189 |
| A | ARG212 |
| A | HIS224 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | binding site for residue 9BG B 301 |
| Chain | Residue |
| A | SER43 |
| A | HIS46 |
| A | GLN47 |
| A | PHE48 |
| A | ARG93 |
| A | ILE146 |
| A | ARG147 |
| A | SER153 |
| A | HOH483 |
| B | SER172 |
| B | VAL173 |
| B | TYR181 |
| B | ILE184 |
| B | LYS185 |
| B | ALA188 |
| B | LEU189 |
| B | ARG212 |
| B | HIS224 |
| B | ARG226 |
| B | HOH415 |
| B | HOH464 |
| B | HOH465 |
| B | HOH474 |
| B | HOH495 |
| B | HOH502 |
| B | HOH532 |
| B | HOH537 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | binding site for residue 9BG C 301 |
| Chain | Residue |
| C | SER172 |
| C | VAL173 |
| C | TYR181 |
| C | ILE184 |
| C | LYS185 |
| C | ARG212 |
| C | ARG226 |
| C | HOH407 |
| C | HOH449 |
| C | HOH453 |
| C | HOH458 |
| C | HOH526 |
| D | SER43 |
| D | TYR45 |
| D | HIS46 |
| D | GLN47 |
| D | PHE48 |
| D | ILE56 |
| D | ARG93 |
| D | ILE146 |
| D | ARG147 |
| D | SER153 |
| D | HIS155 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | binding site for residue 9BG E 301 |
| Chain | Residue |
| F | ARG147 |
| F | SER153 |
| F | HIS155 |
| F | HOH462 |
| F | HOH477 |
| E | SER172 |
| E | VAL173 |
| E | TYR174 |
| E | TYR181 |
| E | ILE184 |
| E | LYS185 |
| E | LEU189 |
| E | ARG212 |
| E | ARG226 |
| E | HOH451 |
| E | HOH487 |
| E | HOH489 |
| E | HOH493 |
| F | SER43 |
| F | TYR45 |
| F | HIS46 |
| F | GLN47 |
| F | PHE48 |
| F | ILE56 |
| F | ARG93 |
| F | ILE146 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | binding site for residue 9BG F 301 |
| Chain | Residue |
| E | TYR45 |
| E | HIS46 |
| E | GLN47 |
| E | PHE48 |
| E | ARG93 |
| E | ILE146 |
| E | ARG147 |
| E | SER153 |
| E | HIS155 |
| E | HOH508 |
| F | SER172 |
| F | VAL173 |
| F | TYR174 |
| F | TYR181 |
| F | ILE184 |
| F | LYS185 |
| F | ALA188 |
| F | LEU189 |
| F | ARG212 |
| F | ARG226 |
| F | HOH405 |
| F | HOH442 |
| F | HOH444 |
| F | HOH455 |
| F | HOH460 |
| F | HOH476 |
| F | HOH493 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | binding site for residue 9BG G 301 |
| Chain | Residue |
| G | SER172 |
| G | VAL173 |
| G | TYR174 |
| G | TYR181 |
| G | LYS185 |
| G | ALA188 |
| G | LEU189 |
| G | ARG212 |
| G | ARG226 |
| G | HOH412 |
| G | HOH448 |
| G | HOH454 |
| G | HOH499 |
| H | SER43 |
| H | TYR45 |
| H | HIS46 |
| H | GLN47 |
| H | PHE48 |
| H | ARG93 |
| H | ILE146 |
| H | ARG147 |
| H | SER153 |
| H | HIS155 |
| H | HOH313 |
| H | HOH366 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | binding site for residue 9BG I 301 |
| Chain | Residue |
| I | SER172 |
| I | VAL173 |
| I | TYR181 |
| I | ILE184 |
| I | LYS185 |
| I | ALA188 |
| I | LEU189 |
| I | ARG212 |
| I | ARG226 |
| I | HOH428 |
| I | HOH434 |
| I | HOH437 |
| I | HOH471 |
| I | HOH494 |
| I | HOH522 |
| I | HOH545 |
| J | SER43 |
| J | HIS46 |
| J | GLN47 |
| J | PHE48 |
| J | ARG93 |
| J | ILE146 |
| J | ARG147 |
| J | SER153 |
| J | HIS155 |
| J | HOH530 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | binding site for residue 9BG J 301 |
| Chain | Residue |
| I | SER43 |
| I | HIS46 |
| I | GLN47 |
| I | PHE48 |
| I | ARG93 |
| I | ILE146 |
| I | ARG147 |
| I | SER153 |
| I | HIS155 |
| I | HOH472 |
| J | SER172 |
| J | VAL173 |
| J | TYR181 |
| J | ILE184 |
| J | LYS185 |
| J | ALA188 |
| J | ARG212 |
| J | HIS224 |
| J | ARG226 |
| J | HOH420 |
| J | HOH429 |
| J | HOH464 |
| J | HOH473 |
| J | HOH531 |
| site_id | AC9 |
| Number of Residues | 26 |
| Details | binding site for residue 9BG K 301 |
| Chain | Residue |
| K | SER172 |
| K | VAL173 |
| K | TYR174 |
| K | TYR181 |
| K | ILE184 |
| K | LYS185 |
| K | ALA188 |
| K | LEU189 |
| K | ARG212 |
| K | ARG226 |
| K | HOH436 |
| K | HOH438 |
| K | HOH459 |
| K | HOH487 |
| K | HOH521 |
| L | SER43 |
| L | TYR45 |
| L | HIS46 |
| L | GLN47 |
| L | PHE48 |
| L | ARG93 |
| L | ILE146 |
| L | ARG147 |
| L | SER153 |
| L | HIS155 |
| L | HOH370 |
| site_id | AD1 |
| Number of Residues | 28 |
| Details | binding site for residue 9BG M 301 |
| Chain | Residue |
| M | SER172 |
| M | VAL173 |
| M | TYR174 |
| M | TYR181 |
| M | LYS185 |
| M | ALA188 |
| M | LEU189 |
| M | ARG212 |
| M | ARG226 |
| M | HOH412 |
| M | HOH454 |
| M | HOH464 |
| M | HOH467 |
| M | HOH477 |
| M | HOH478 |
| M | HOH497 |
| N | SER43 |
| N | TYR45 |
| N | HIS46 |
| N | GLN47 |
| N | PHE48 |
| N | ILE56 |
| N | ARG93 |
| N | ILE146 |
| N | ARG147 |
| N | SER153 |
| N | HIS155 |
| N | HOH375 |
| site_id | AD2 |
| Number of Residues | 24 |
| Details | binding site for residue 9BG M 302 |
| Chain | Residue |
| M | TYR45 |
| M | HIS46 |
| M | GLN47 |
| M | PHE48 |
| M | ARG93 |
| M | ILE146 |
| M | ARG147 |
| M | SER153 |
| M | HIS155 |
| M | HOH406 |
| M | HOH430 |
| M | HOH456 |
| M | HOH485 |
| N | SER172 |
| N | VAL173 |
| N | TYR174 |
| N | TYR181 |
| N | ILE184 |
| N | LYS185 |
| N | ALA188 |
| N | LEU189 |
| N | ARG212 |
| N | ARG226 |
| N | HOH338 |
| site_id | AD3 |
| Number of Residues | 24 |
| Details | binding site for residue 9BG P 301 |
| Chain | Residue |
| O | SER172 |
| O | VAL173 |
| O | TYR181 |
| O | LYS185 |
| O | ALA188 |
| O | LEU189 |
| O | ARG212 |
| O | ARG226 |
| O | HOH347 |
| O | HOH374 |
| P | TYR45 |
| P | HIS46 |
| P | GLN47 |
| P | PHE48 |
| P | ARG93 |
| P | ILE146 |
| P | ARG147 |
| P | SER153 |
| P | HIS155 |
| P | HOH421 |
| P | HOH429 |
| P | HOH469 |
| P | HOH481 |
| P | HOH496 |
| site_id | AD4 |
| Number of Residues | 24 |
| Details | binding site for residue 9BG P 302 |
| Chain | Residue |
| O | SER43 |
| O | HIS46 |
| O | GLN47 |
| O | PHE48 |
| O | ILE56 |
| O | ARG93 |
| O | ILE146 |
| O | ARG147 |
| O | SER153 |
| O | HIS155 |
| O | HOH360 |
| P | SER172 |
| P | VAL173 |
| P | TYR181 |
| P | LYS185 |
| P | ALA188 |
| P | LEU189 |
| P | ARG212 |
| P | HIS224 |
| P | ARG226 |
| P | HOH411 |
| P | HOH458 |
| P | HOH466 |
| P | HOH521 |
| site_id | AD5 |
| Number of Residues | 31 |
| Details | binding site for Di-peptide 9BG C 302 and ARG C 93 |
| Chain | Residue |
| C | TYR45 |
| C | HIS46 |
| C | GLN47 |
| C | PHE48 |
| C | VAL89 |
| C | CYS90 |
| C | ASN91 |
| C | LYS92 |
| C | PHE94 |
| C | VAL95 |
| C | ILE146 |
| C | ARG147 |
| C | SER153 |
| C | HIS155 |
| C | HOH415 |
| C | HOH422 |
| C | HOH445 |
| C | HOH447 |
| C | HOH488 |
| C | HOH502 |
| C | HOH507 |
| D | SER172 |
| D | VAL173 |
| D | TYR181 |
| D | ILE184 |
| D | LYS185 |
| D | ALA188 |
| D | LEU189 |
| D | ARG212 |
| D | ARG226 |
| D | HOH315 |
| site_id | AD6 |
| Number of Residues | 28 |
| Details | binding site for Di-peptide 9BG G 302 and ARG G 93 |
| Chain | Residue |
| G | HIS46 |
| G | GLN47 |
| G | PHE48 |
| G | VAL89 |
| G | CYS90 |
| G | ASN91 |
| G | LYS92 |
| G | PHE94 |
| G | VAL95 |
| G | ILE146 |
| G | ARG147 |
| G | SER153 |
| G | HIS155 |
| G | HOH403 |
| G | HOH429 |
| G | HOH442 |
| G | HOH462 |
| G | HOH463 |
| G | HOH482 |
| G | HOH522 |
| H | SER172 |
| H | VAL173 |
| H | TYR181 |
| H | LYS185 |
| H | ALA188 |
| H | LEU189 |
| H | ARG212 |
| H | ARG226 |
| site_id | AD7 |
| Number of Residues | 28 |
| Details | binding site for Di-peptide 9BG K 302 and ARG K 93 |
| Chain | Residue |
| K | TYR45 |
| K | HIS46 |
| K | GLN47 |
| K | PHE48 |
| K | VAL89 |
| K | CYS90 |
| K | ASN91 |
| K | LYS92 |
| K | PHE94 |
| K | VAL95 |
| K | ILE146 |
| K | ARG147 |
| K | SER153 |
| K | HIS155 |
| K | HOH443 |
| K | HOH475 |
| K | HOH491 |
| K | HOH496 |
| L | SER172 |
| L | VAL173 |
| L | TYR174 |
| L | TYR181 |
| L | ILE184 |
| L | LYS185 |
| L | ALA188 |
| L | LEU189 |
| L | ARG212 |
| L | ARG226 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_04143","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Active site: {"description":"Shared with catalytic histidine of dimeric partner","evidences":[{"source":"HAMAP-Rule","id":"MF_04143","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Active site: {"description":"Proton acceptor; shared with catalytic histidine of dimeric partner","evidences":[{"source":"HAMAP-Rule","id":"MF_04143","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 48 |
| Details | Site: {"description":"Substrate binding","evidences":[{"source":"HAMAP-Rule","id":"MF_04143","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






