Structure of PDB 1zbh Chain D Binding Site BS03
Receptor Information
>1zbh Chain D (length=289) Species:
9606
(Homo sapiens) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
DFSDPVYKEIAITNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNY
YKKQKLMLKESNFADSYYDYICIIDFEATCEEGNPPEFVHEIIEFPVVLL
NTHTLEIEDTFQQYVRPEINTQLSDFCISLTGITQDQVDRADTFPQVLKK
VIDLMKLKELGTKYKYSLLTDGSWDMSKFLNIQCQLSRLKYPPFAKKWIN
IRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPNCGLDDSKNIARIAVRM
LQDGCELRINEKMHAGQLMSVSSSLPIEGTPPPQMPHFR
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1zbh Chain D Residue 4001 [
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
1zbh
Structural basis for 3'-end specific recognition of histone mRNA stem-loop by 3'-exonuclease, a human nuclease that also targets siRNA
Resolution
3.0 Å
Binding residue
(original residue number in PDB)
D134 E136 D298
Binding residue
(residue number reindexed from 1)
D75 E77 D239
Annotation score
4
Enzymatic activity
Catalytic site (original residue number in PDB)
D134 E136 D234 N293 D298
Catalytic site (residue number reindexed from 1)
D75 E77 D175 N234 D239
Enzyme Commision number
3.1.-.-
Gene Ontology
Molecular Function
GO:0000175
3'-5'-RNA exonuclease activity
GO:0003676
nucleic acid binding
View graph for
Molecular Function
External links
PDB
RCSB:1zbh
,
PDBe:1zbh
,
PDBj:1zbh
PDBsum
1zbh
PubMed
UniProt
Q8IV48
|ERI1_HUMAN 3'-5' exoribonuclease 1 (Gene Name=ERI1)
[
Back to BioLiP
]