Structure of PDB 5edv Chain B Binding Site BS05
Receptor Information
>5edv Chain B (length=333) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
CAVCGWALPHNRMQALTSCECTICPDCFRQHFTIALKEKHITDMVCPACG
RPDLTDSYFSTLDIQLRESLEPDAYALFHKKLTEGVLMRDPKFLWCAQCS
FGFIYEREQLEATCPQCHQTFCVRCKRQWEEQHRGRSCEDFQNWKRMNDP
EYQAQGLAMYLQENGIDCPKCKFSYALARGGCMHFHCTQCRHQFCSGCYN
AFYAKNKCPEPNCRVKKSLHGHHPRDCLFYLRDWTALRLQKLLQDNNVMF
NTEPGGCRVIEQKEVPNGLRDEACGKETPAGYAGLCQAHYKEYLVSLINA
HSLTLYEVEELETATERYLHLQKLTEEVPLGQS
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
5edv Chain B Residue 2005 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
5edv
Structure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation.
Resolution
3.48 Å
Binding residue
(original residue number in PDB)
C871 C874 C890 C893
Binding residue
(residue number reindexed from 1)
C168 C171 C187 C190
Annotation score
4
Enzymatic activity
Enzyme Commision number
2.3.2.31
: RBR-type E3 ubiquitin transferase.
Gene Ontology
Molecular Function
GO:0004842
ubiquitin-protein transferase activity
GO:0008270
zinc ion binding
Cellular Component
GO:0071797
LUBAC complex
View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB
RCSB:5edv
,
PDBe:5edv
,
PDBj:5edv
PDBsum
5edv
PubMed
26789245
UniProt
Q96EP0
|RNF31_HUMAN E3 ubiquitin-protein ligase RNF31 (Gene Name=RNF31)
[
Back to BioLiP
]