Structure of PDB 5vo3 Chain A Binding Site BS03
Receptor Information
>5vo3 Chain A (length=380) Species:
727
(Haemophilus influenzae) [
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ASNAMKEKVVSLAQDLIRRPSISPNDEGCQQIIAERLEKLGFQIEWMPFN
DTLNLWAKHGTSEPVIAFAGHTDVVPTGDENQWSSPPFSAEIIDGMLYGR
GAADMKGSLAAMIVAAEEYVKANPNHKGTIALLITSDEEATAKDGTIHVV
ETLMARDEKITYCMVGEPSSAKNLGDVVKNGRRGSITGNLYIQGIQGHVA
YPHLAENPIHKAALFLQELTTYQWDKGNEFFPPTSLQIANIHAGTGSNNV
IPAELYIQFNLRYCTEVTDEIIKQKVAEMLEKHNLKYRIEWNLSGKPFLT
KPGKLLDSITSAIEETIGITPKAETGGGTSDGRFIALMGAEVVEFGPLNS
TIHKVNECVSVEDLGKCGEIYHKMLVNLLD
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
5vo3 Chain A Residue 503 [
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Receptor-Ligand Complex Structure
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PDB
5vo3
Structural Evidence of a Major Conformational Change Triggered by Substrate Binding in DapE Enzymes: Impact on the Catalytic Mechanism.
Resolution
1.954 Å
Binding residue
(original residue number in PDB)
H67 D100 E163
Binding residue
(residue number reindexed from 1)
H71 D104 E167
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.5.1.18
: succinyl-diaminopimelate desuccinylase.
Gene Ontology
Molecular Function
GO:0008270
zinc ion binding
GO:0009014
succinyl-diaminopimelate desuccinylase activity
GO:0016787
hydrolase activity
GO:0046872
metal ion binding
GO:0050897
cobalt ion binding
Biological Process
GO:0009085
lysine biosynthetic process
GO:0009089
lysine biosynthetic process via diaminopimelate
GO:0019877
diaminopimelate biosynthetic process
Cellular Component
GO:0005829
cytosol
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:5vo3
,
PDBe:5vo3
,
PDBj:5vo3
PDBsum
5vo3
PubMed
29272107
UniProt
P44514
|DAPE_HAEIN Succinyl-diaminopimelate desuccinylase (Gene Name=dapE)
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