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6APX

Crystal structure of human dual specificity phosphatase 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the monobody YSX1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0006470biological_processprotein dephosphorylation
A0006974biological_processDNA damage response
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0016311biological_processdephosphorylation
A0030288cellular_componentouter membrane-bounded periplasmic space
A0034219biological_processcarbohydrate transmembrane transport
A0034289biological_processdetection of maltose stimulus
A0042597cellular_componentperiplasmic space
A0042956biological_processmaltodextrin transmembrane transport
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A0071702biological_processorganic substance transport
A1901982molecular_functionmaltose binding
A1990060cellular_componentmaltose transport complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 1401
ChainResidue
AGLY1172
AHIS1188
AARG1292

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 1402
ChainResidue
AARG1264
AHOH1513
ASER1258
AGLN1259
AALA1260
AGLY1261
AILE1262
ASER1263

site_idAC3
Number of Residues8
Detailsbinding site for residue SO4 A 1403
ChainResidue
AGLN72
ASER1207
AALA1208
AASN1209
ACYS1210
AGLU1226
AGLN1259
AARG1264

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL A 1404
ChainResidue
AALA172
AALA173

Functional Information from PROSITE/UniProt
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO107-ASN124

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP
ChainResidueDetails
BGLY37-PRO44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Phosphocysteine intermediate => ECO:0000255|PROSITE-ProRule:PRU00160
ChainResidueDetails
ASER1258

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PDB entries from 2024-06-12

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