6D66
Crystal structure of the human dual specificity 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein mbp3_16
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0006974 | biological_process | DNA damage response |
A | 0008643 | biological_process | carbohydrate transport |
A | 0015144 | molecular_function | carbohydrate transmembrane transporter activity |
A | 0015768 | biological_process | maltose transport |
A | 0016020 | cellular_component | membrane |
A | 0016311 | biological_process | dephosphorylation |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0034219 | biological_process | carbohydrate transmembrane transport |
A | 0034289 | biological_process | detection of maltose stimulus |
A | 0042597 | cellular_component | periplasmic space |
A | 0042956 | biological_process | maltodextrin transmembrane transport |
A | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
A | 0055052 | cellular_component | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing |
A | 0055085 | biological_process | transmembrane transport |
A | 0060326 | biological_process | cell chemotaxis |
A | 0071702 | biological_process | organic substance transport |
A | 1901982 | molecular_function | maltose binding |
A | 1990060 | cellular_component | maltose transport complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue PEG A 1401 |
Chain | Residue |
A | GLU154 |
A | EDO1407 |
A | EDO1419 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue PO4 A 1402 |
Chain | Residue |
A | SER463 |
A | ARG464 |
A | HOH1649 |
A | ASP427 |
A | SER458 |
A | GLN459 |
A | ALA460 |
A | GLY461 |
A | ILE462 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue GLY A 1403 |
Chain | Residue |
A | ALA325 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue PGE A 1404 |
Chain | Residue |
A | TYR91 |
A | GLN326 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue EDO A 1405 |
Chain | Residue |
A | LYS430 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue EDO A 1406 |
Chain | Residue |
A | GLN419 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 1407 |
Chain | Residue |
A | ASP66 |
A | MET331 |
A | PEG1401 |
A | HOH1506 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue PG4 A 1408 |
Chain | Residue |
A | ALA84 |
A | GLN87 |
B | LYS68 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue EDO A 1409 |
Chain | Residue |
A | ASN350 |
A | ARG355 |
A | ARG453 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO A 1410 |
Chain | Residue |
A | SER496 |
A | PRO497 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue PGE A 1411 |
Chain | Residue |
A | LYS128 |
A | SER390 |
A | LYS392 |
A | ASP393 |
A | PHE414 |
A | HOH1536 |
A | HOH1686 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue GLY A 1412 |
Chain | Residue |
A | ASP482 |
A | MET502 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue GLY A 1413 |
Chain | Residue |
A | SER435 |
A | GLU439 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 1414 |
Chain | Residue |
A | ASP96 |
A | TYR177 |
A | ILE330 |
A | HOH1513 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue PGE A 1415 |
Chain | Residue |
A | ASN283 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue EDO A 1416 |
Chain | Residue |
A | GLU292 |
A | TYR308 |
A | HIS519 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue PEG A 1417 |
Chain | Residue |
A | GLU279 |
A | GLU282 |
A | HOH1545 |
B | ASN36 |
site_id | AD9 |
Number of Residues | 1 |
Details | binding site for residue EDO A 1418 |
Chain | Residue |
A | ASP427 |
site_id | AE1 |
Number of Residues | 1 |
Details | binding site for residue EDO A 1419 |
Chain | Residue |
A | PEG1401 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue EDO B 201 |
Chain | Residue |
A | TYR387 |
A | GLN459 |
B | ASP122 |
B | HOH363 |
site_id | AE3 |
Number of Residues | 1 |
Details | binding site for residue EDO B 202 |
Chain | Residue |
B | HIS23 |
site_id | AE4 |
Number of Residues | 2 |
Details | binding site for residue PEG B 203 |
Chain | Residue |
B | GLU64 |
B | LYS101 |
site_id | AE5 |
Number of Residues | 3 |
Details | binding site for residue DAL B 204 |
Chain | Residue |
A | ALA85 |
B | ARG31 |
B | TYR69 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 205 |
Chain | Residue |
B | GLN26 |
B | ASP27 |
B | ASP28 |
B | GLU29 |
Functional Information from PROSITE/UniProt
site_id | PS01037 |
Number of Residues | 18 |
Details | SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN |
Chain | Residue | Details |
A | PRO108-ASN125 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160 |
Chain | Residue | Details |
A | SER458 |