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2RR9

The solution structure of the K63-Ub2:tUIMs complex

Functional Information from GO Data
ChainGOidnamespacecontents
C0006302biological_processdouble-strand break repair
C0070530molecular_functionK63-linked polyubiquitin modification-dependent protein binding
C0070531cellular_componentBRCA1-A complex
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
ALYS27-ASP52

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues150
DetailsDomain: {"description":"Ubiquitin-like 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues19
DetailsDomain: {"description":"UIM 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00213","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues19
DetailsDomain: {"description":"UIM 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00213","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsRegion: {"description":"UIM-linker"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525341","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17525342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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