Structure of PDB 1kgz Chain B Binding Site BS02
Receptor Information
>1kgz Chain B (length=330) Species:
554
(Pectobacterium carotovorum) [
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THQPILEKLFKSQSMTQEESHQLFAAIVRGELEDSQLAAALISMKMRGER
PEEIAGAASALLADAQPFPRPDYDFADIVGTGGDGTNSINISTASAFVAA
SCGAKVAKHGNRSVLAGSCDLLQAFGIRLDMSAEDSRQALDDLNVCFLFA
PQYHTGFRHAMPVRQQLKTRTIFNVLGPLINPARPPKALIGVYSPELVLP
IAQALKVLGYKNAAVVHGGGMDEVAIHTPTQVAELNNGEIESYQLSPQDF
GLQSYSLNALQGGTPEENRDILARLLQGKGDAAHARQVAANVALLLKLFG
QDNLRHNAQLALETIRSGTAFERVTALAAR
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1kgz Chain B Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
1kgz
The Crystal Structure of Anthranilate Phosphoribosyltransferase from the Enterobacterium Pectobacterium carotovorum
Resolution
2.4 Å
Binding residue
(original residue number in PDB)
D236 E237
Binding residue
(residue number reindexed from 1)
D222 E223
Annotation score
1
Enzymatic activity
Enzyme Commision number
2.4.2.18
: anthranilate phosphoribosyltransferase.
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0004048
anthranilate phosphoribosyltransferase activity
GO:0016757
glycosyltransferase activity
GO:0016763
pentosyltransferase activity
GO:0046872
metal ion binding
Biological Process
GO:0000162
tryptophan 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:1kgz
,
PDBe:1kgz
,
PDBj:1kgz
PDBsum
1kgz
PubMed
12123839
UniProt
Q8VP84
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