Structure of PDB 1d00 Chain A

Receptor sequence
>1d00A (length=168) Species: 9606 (Homo sapiens) [Search protein sequence]
AMADLEQKVLEMEASTYDGVFIWKISDFARKRQEAVAGRIPAIFSPAFYT
SRYGYKMCLRIYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLM
LLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFCPVSKMEAKNS
YVRDDAIFIKAIVDLTGL
3D structure
PDB1d00 The structural basis for the recognition of diverse receptor sequences by TRAF2.
ChainA
Resolution2.0 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 A R393 Y395 D399 F410 F447 S455 I465 A466 S467 G468 R60 Y62 D66 F77 F114 S122 I132 A133 S134 G135
Gene Ontology
Molecular Function
GO:0004842 ubiquitin-protein transferase activity
GO:0005164 tumor necrosis factor receptor binding
Biological Process
GO:0007250 activation of NF-kappaB-inducing kinase activity
GO:0033209 tumor necrosis factor-mediated signaling pathway
GO:0042981 regulation of apoptotic process
GO:0046328 regulation of JNK cascade
GO:0051865 protein autoubiquitination

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1d00, PDBe:1d00, PDBj:1d00
PDBsum1d00
PubMed10518213
UniProtQ12933|TRAF2_HUMAN TNF receptor-associated factor 2 (Gene Name=TRAF2)

[Back to BioLiP]