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7CY7

Crystal Structure of CMD1 in complex with DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0006211biological_process5-methylcytosine catabolic process
A0006974biological_processDNA damage response
A0008643biological_processcarbohydrate transport
A0010109biological_processregulation of photosynthesis
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
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A0071702biological_processorganic substance transport
A0120204molecular_functionmethylcytosine to 5-glyceryl-methylcytosine dioxygenase activity
A1901982molecular_functionmaltose binding
A1990060cellular_componentmaltose transport complex
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. IAGGEFVLPSLGISF
ChainResidueDetails
AILE366-PHE380

site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GELSGKAT
ChainResidueDetails
AGLY201-THR208

site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO-266-ASN-249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:33531488, ECO:0007744|PDB:7CY5, ECO:0007744|PDB:7CY8
ChainResidueDetails
ASER335

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:33531488, ECO:0000305|PubMed:31043749
ChainResidueDetails
AASP347
AHIS345

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:33531488
ChainResidueDetails
AHIS397

220472

PDB entries from 2024-05-29

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