Structure of PDB 1kgz Chain B Binding Site BS02

Receptor Information
>1kgz Chain B (length=330) Species: 554 (Pectobacterium carotovorum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
THQPILEKLFKSQSMTQEESHQLFAAIVRGELEDSQLAAALISMKMRGER
PEEIAGAASALLADAQPFPRPDYDFADIVGTGGDGTNSINISTASAFVAA
SCGAKVAKHGNRSVLAGSCDLLQAFGIRLDMSAEDSRQALDDLNVCFLFA
PQYHTGFRHAMPVRQQLKTRTIFNVLGPLINPARPPKALIGVYSPELVLP
IAQALKVLGYKNAAVVHGGGMDEVAIHTPTQVAELNNGEIESYQLSPQDF
GLQSYSLNALQGGTPEENRDILARLLQGKGDAAHARQVAANVALLLKLFG
QDNLRHNAQLALETIRSGTAFERVTALAAR
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain1kgz Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1kgz The Crystal Structure of Anthranilate Phosphoribosyltransferase from the Enterobacterium Pectobacterium carotovorum
Resolution2.4 Å
Binding residue
(original residue number in PDB)
D236 E237
Binding residue
(residue number reindexed from 1)
D222 E223
Annotation score1
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
PDBsum1kgz
PubMed12123839
UniProtQ8VP84

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