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4EGC

Crystal Structure of MBP-fused Human Six1 Bound to Human Eya2 Eya Domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0000981molecular_functionDNA-binding transcription factor activity, RNA polymerase II-specific
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0006355biological_processregulation of DNA-templated transcription
A0006974biological_processDNA damage response
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
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_processobsolete organic substance transport
A1901982molecular_functionmaltose binding
A1990060cellular_componentmaltose transport complex
B0004725molecular_functionprotein tyrosine phosphatase activity
B0007275biological_processmulticellular organism development
Functional Information from PROSITE/UniProt
site_idPS00027
Number of Residues24
DetailsHOMEOBOX_1 'Homeobox' domain signature. LAeaTgLTttQVSNWFkNrrqrdR
ChainResidueDetails
ALEU527-ARG550

site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO107-ASN124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:19858093
ChainResidueDetails
BASP274

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:19858093
ChainResidueDetails
BASP276

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19351884
ChainResidueDetails
BASP274
BASP276
BASP502

221716

PDB entries from 2024-06-26

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