2V0N
ACTIVATED RESPONSE REGULATOR PLED IN COMPLEX WITH C-DIGMP AND GTP- ALPHA-S
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000160 | biological_process | phosphorelay signal transduction system |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0016740 | molecular_function | transferase activity |
A | 0030154 | biological_process | cell differentiation |
A | 0043709 | biological_process | cell adhesion involved in single-species biofilm formation |
A | 0046872 | molecular_function | metal ion binding |
A | 0052621 | molecular_function | diguanylate cyclase activity |
A | 1902201 | biological_process | negative regulation of bacterial-type flagellum-dependent cell motility |
B | 0000160 | biological_process | phosphorelay signal transduction system |
B | 0005525 | molecular_function | GTP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005886 | cellular_component | plasma membrane |
B | 0016740 | molecular_function | transferase activity |
B | 0030154 | biological_process | cell differentiation |
B | 0043709 | biological_process | cell adhesion involved in single-species biofilm formation |
B | 0046872 | molecular_function | metal ion binding |
B | 0052621 | molecular_function | diguanylate cyclase activity |
B | 1902201 | biological_process | negative regulation of bacterial-type flagellum-dependent cell motility |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BEF A 501 |
Chain | Residue |
A | ASP53 |
A | VAL54 |
A | MET55 |
A | THR83 |
A | ALA84 |
A | LYS105 |
A | MG502 |
A | HOH2001 |
B | GLU423 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | ASP10 |
A | ASP53 |
A | MET55 |
A | BEF501 |
A | HOH2001 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE C2E A 503 |
Chain | Residue |
A | ARG359 |
A | ASP362 |
A | ASP383 |
A | ARG386 |
A | ILE387 |
A | ARG390 |
A | C2E505 |
B | ARG313 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE C2E A 505 |
Chain | Residue |
A | ASN357 |
A | VAL358 |
A | ARG359 |
A | ALA360 |
A | ARG390 |
A | C2E503 |
B | SER309 |
B | LYS312 |
B | ARG313 |
B | GLY318 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE GAV A 600 |
Chain | Residue |
A | ASP327 |
A | ILE328 |
A | ASP329 |
A | PHE330 |
A | PHE331 |
A | LYS332 |
A | ASN335 |
A | HIS340 |
A | ASP344 |
A | ARG366 |
A | GLY369 |
A | GLU370 |
A | LYS442 |
A | ARG446 |
A | MG601 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 601 |
Chain | Residue |
A | ASP327 |
A | ILE328 |
A | GLU370 |
A | GAV600 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 602 |
Chain | Residue |
A | ASP327 |
A | GLU370 |
A | GLU371 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BEF B 501 |
Chain | Residue |
B | ASP53 |
B | VAL54 |
B | MET55 |
B | THR83 |
B | ALA84 |
B | LYS105 |
B | MG502 |
B | HOH2001 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 502 |
Chain | Residue |
B | ASP10 |
B | ASP53 |
B | MET55 |
B | BEF501 |
B | HOH2001 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE C2E B 503 |
Chain | Residue |
A | ARG313 |
B | ARG359 |
B | ASP362 |
B | ASP383 |
B | ARG386 |
B | ILE387 |
B | ARG390 |
B | C2E505 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE C2E B 505 |
Chain | Residue |
A | SER309 |
A | ARG313 |
A | GLY318 |
B | ASN357 |
B | VAL358 |
B | ARG359 |
B | ARG390 |
B | C2E503 |
site_id | BC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GAV B 600 |
Chain | Residue |
A | GLY144 |
A | ALA145 |
B | ASP327 |
B | ILE328 |
B | PHE330 |
B | PHE331 |
B | LYS332 |
B | ASN335 |
B | HIS340 |
B | ASP344 |
B | ARG366 |
B | GLY369 |
B | GLU370 |
B | LYS442 |
B | ARG446 |
B | MG601 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 601 |
Chain | Residue |
B | ASP327 |
B | ILE328 |
B | GLU370 |
B | LYS442 |
B | GAV600 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 1470 |
Chain | Residue |
A | ASN162 |
A | ARG164 |
A | ARG168 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 1471 |
Chain | Residue |
A | ARG117 |
A | ARG121 |
B | ARG117 |
B | ARG121 |
site_id | BC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 1472 |
Chain | Residue |
A | ARG386 |
A | ALA419 |
A | ALA421 |
A | ALA453 |
A | ALA454 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255 |
Chain | Residue | Details |
A | GLU370 | |
B | GLU370 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15569936 |
Chain | Residue | Details |
A | ASP9 | |
B | ASP9 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15569936, ECO:0000269|PubMed:17697997, ECO:0000269|Ref.6 |
Chain | Residue | Details |
A | ASP10 | |
A | ASP53 | |
A | MET55 | |
B | ASP10 | |
B | ASP53 | |
B | MET55 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:15569936, ECO:0000305|Ref.6 |
Chain | Residue | Details |
A | ASN335 | |
A | ASP344 | |
B | ASN335 | |
B | ASP344 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Allosteric product binding, non-activate state |
Chain | Residue | Details |
A | ARG178 | |
B | ARG178 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000255 |
Chain | Residue | Details |
A | LYS332 | |
B | LYS332 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | SITE: Allosteric product phosphate group binding, activate and inactive state |
Chain | Residue | Details |
A | ARG359 | |
B | ARG359 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | SITE: Allosteric product binding, activate and inactive state |
Chain | Residue | Details |
A | ASP362 | |
A | ARG390 | |
B | ASP362 | |
B | ARG390 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:12622822, ECO:0000269|PubMed:15075296 |
Chain | Residue | Details |
A | ASP53 | |
B | ASP53 |
site_id | SWS_FT_FI10 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17697997 |
Chain | Residue | Details |
A | ASP327 | |
A | ILE328 | |
A | GLU370 | |
B | ASP327 | |
B | ILE328 | |
B | GLU370 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | SITE: Allosteric product binding, active state |
Chain | Residue | Details |
A | ARG313 | |
B | ARG313 |