Structure of PDB 1t2v Chain D

Receptor sequence
>1t2vD (length=205) Species: 9606 (Homo sapiens) [Search protein sequence]
NKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFV
CERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNH
QGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELS
SFTLGTGVHPIVVVQPDAWTFHAIGQMCAPVVTREWVLDSVALYQCQELD
TYLIP
3D structure
PDB1t2v Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1
ChainD
Resolution3.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 2.3.2.27: RING-type E3 ubiquitin transferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide D S1655 P1659 E1698 R1699 T1700 K1702 N1774 M1775 S9 P13 E52 R53 T54 K56 N128 M129
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0004842 ubiquitin-protein transferase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006281 DNA repair
GO:0006974 DNA damage response
Cellular Component
GO:0005634 nucleus

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1t2v, PDBe:1t2v, PDBj:1t2v
PDBsum1t2v
PubMed15133503
UniProtP38398|BRCA1_HUMAN Breast cancer type 1 susceptibility protein (Gene Name=BRCA1)

[Back to BioLiP]