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 | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
B | 0004518 | molecular_function | nuclease activity |
B | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
C | 0004518 | molecular_function | nuclease activity |
C | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
D | 0004518 | molecular_function | nuclease activity |
D | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
E | 0004518 | molecular_function | nuclease activity |
E | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
F | 0004518 | molecular_function | nuclease activity |
F | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
G | 0004518 | molecular_function | nuclease activity |
G | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
H | 0004518 | molecular_function | nuclease activity |
H | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
I | 0004518 | molecular_function | nuclease activity |
I | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
J | 0004518 | molecular_function | nuclease activity |
J | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
K | 0004518 | molecular_function | nuclease activity |
K | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
L | 0004518 | molecular_function | nuclease activity |
L | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
M | 0004518 | molecular_function | nuclease activity |
M | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
N | 0004518 | molecular_function | nuclease activity |
N | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
O | 0004518 | molecular_function | nuclease activity |
O | 0061507 | molecular_function | 2',3'-cyclic GMP-AMP binding |
P | 0004518 | molecular_function | nuclease 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 | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_04143 |
Chain | Residue | Details |
A | HIS46 | |
J | HIS46 | |
K | HIS46 | |
L | HIS46 | |
M | HIS46 | |
N | HIS46 | |
O | HIS46 | |
P | HIS46 | |
B | HIS46 | |
C | HIS46 | |
D | HIS46 | |
E | HIS46 | |
F | HIS46 | |
G | HIS46 | |
H | HIS46 | |
I | HIS46 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | ACT_SITE: Shared with catalytic histidine of dimeric partner => ECO:0000255|HAMAP-Rule:MF_04143 |
Chain | Residue | Details |
A | TYR181 | |
J | TYR181 | |
K | TYR181 | |
L | TYR181 | |
M | TYR181 | |
N | TYR181 | |
O | TYR181 | |
P | TYR181 | |
B | TYR181 | |
C | TYR181 | |
D | TYR181 | |
E | TYR181 | |
F | TYR181 | |
G | TYR181 | |
H | TYR181 | |
I | TYR181 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | ACT_SITE: Proton acceptor; shared with catalytic histidine of dimeric partner => ECO:0000255|HAMAP-Rule:MF_04143 |
Chain | Residue | Details |
A | LYS185 | |
J | LYS185 | |
K | LYS185 | |
L | LYS185 | |
M | LYS185 | |
N | LYS185 | |
O | LYS185 | |
P | LYS185 | |
B | LYS185 | |
C | LYS185 | |
D | LYS185 | |
E | LYS185 | |
F | LYS185 | |
G | LYS185 | |
H | LYS185 | |
I | LYS185 |
site_id | SWS_FT_FI4 |
Number of Residues | 48 |
Details | SITE: Substrate binding => ECO:0000255|HAMAP-Rule:MF_04143 |
Chain | Residue | Details |
A | ARG93 | |
D | ARG93 | |
D | ILE146 | |
D | ARG226 | |
E | ARG93 | |
E | ILE146 | |
E | ARG226 | |
F | ARG93 | |
F | ILE146 | |
F | ARG226 | |
G | ARG93 | |
A | ILE146 | |
G | ILE146 | |
G | ARG226 | |
H | ARG93 | |
H | ILE146 | |
H | ARG226 | |
I | ARG93 | |
I | ILE146 | |
I | ARG226 | |
J | ARG93 | |
J | ILE146 | |
A | ARG226 | |
J | ARG226 | |
K | ARG93 | |
K | ILE146 | |
K | ARG226 | |
L | ARG93 | |
L | ILE146 | |
L | ARG226 | |
M | ARG93 | |
M | ILE146 | |
M | ARG226 | |
B | ARG93 | |
N | ARG93 | |
N | ILE146 | |
N | ARG226 | |
O | ARG93 | |
O | ILE146 | |
O | ARG226 | |
P | ARG93 | |
P | ILE146 | |
P | ARG226 | |
B | ILE146 | |
B | ARG226 | |
C | ARG93 | |
C | ILE146 | |
C | ARG226 |