Structure of PDB 5uej Chain B Binding Site BS02
Receptor Information
>5uej Chain B (length=376) Species:
487
(Neisseria meningitidis) [
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TETQSLELAKELISRPSVTPDDRDCQKLLAERLHKIGFAAEELHFGDTKN
IWLRRGTKAPVVCFAGHTDVVPTGPVEKWDSPPFEPAERDGRLYGRGAAD
MKTSIACFVTACERFVAKHPNHQGSIALLITSDEEGDALDGTTKVVDVLK
ARDELIDYCIVGEPTAVDKLGDMIKNGRRGSLSGNLTVKGKQGHIAYPHL
AINPVHTFAPALLELTQEVWDEGNEYFPPTSFQISNINGGTGATNVIPGE
LNVKFNFRFSTESTEAGLKQRVHAILDKHGVQYDLQWSCSGQPFLTQAGK
LTDVARAAIAETCGIEAELSTTGGTSDGRFIKAIAQELIELGPSNATIHQ
INENVRLNDIPKLSAVYEGILARLLA
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
5uej Chain B Residue 402 [
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Receptor-Ligand Complex Structure
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PDB
5uej
1.30 A crystal structure of DapE enzyme from Neisseria meningitidis MC58
Resolution
1.3 Å
Binding residue
(original residue number in PDB)
H68 D101 E164
Binding residue
(residue number reindexed from 1)
H67 D100 E163
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:0008777
acetylornithine deacetylase activity
GO:0009014
succinyl-diaminopimelate desuccinylase activity
GO:0016787
hydrolase activity
GO:0046872
metal ion binding
GO:0050897
cobalt ion binding
Biological Process
GO:0006526
L-arginine biosynthetic process
GO:0009085
lysine biosynthetic process
GO:0009089
lysine biosynthetic process via diaminopimelate
GO:0019877
diaminopimelate biosynthetic process
View graph for
Molecular Function
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Biological Process
External links
PDB
RCSB:5uej
,
PDBe:5uej
,
PDBj:5uej
PDBsum
5uej
PubMed
UniProt
Q9JYL2
|DAPE_NEIMB Succinyl-diaminopimelate desuccinylase (Gene Name=dapE)
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