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4K7R

Crystal structures of CusC review conformational changes accompanying folding and transmembrane channel formation

Functional Information from GO Data
ChainGOidnamespacecontents
A0005375molecular_functioncopper ion transmembrane transporter activity
A0005507molecular_functioncopper ion binding
A0005515molecular_functionprotein binding
A0006811biological_processmonoatomic ion transport
A0006878biological_processintracellular copper ion homeostasis
A0009279cellular_componentcell outer membrane
A0009636biological_processresponse to toxic substance
A0010272biological_processresponse to silver ion
A0010273biological_processdetoxification of copper ion
A0015288molecular_functionporin activity
A0015562molecular_functionefflux transmembrane transporter activity
A0016020cellular_componentmembrane
A0019992molecular_functiondiacylglycerol binding
A0022857molecular_functiontransmembrane transporter activity
A0035434biological_processcopper ion transmembrane transport
A0042802molecular_functionidentical protein binding
A0046688biological_processresponse to copper ion
A0046930cellular_componentpore complex
A0055085biological_processtransmembrane transport
A0060003biological_processcopper ion export
A0070207biological_processprotein homotrimerization
A1902601biological_processsilver ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 3PK A 501
ChainResidue
ACYS1
APHE119
AILE291

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsLipidation: {"description":"S-diacylglycerol cysteine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00303","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21249122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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