Structure of PDB 2o18 Chain C Binding Site BS01

Receptor Information

>2o18 Chain C (length=313) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

TEVTVLEGKTMGTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTYKK
DSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNL
WGFGPEQQPVQIPSQEQIDAMKAKTGLQHLTVINQSHQQYLQKDLPDLYV
DLSTVGEGYAADHLARLMEQEGISRYLVSVGGALNSRGMNGEGLPWRVAI
QKPTVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLV
SVTVIAPTALEADAWDTGLMVLGPEKAKEVVRREGLAVYMITKEGDSFKT
WMSPQFKSFLVSE

Ligand information

Ligand ID

InChI

InChI=1S/Ca/q+2

InChIKey

BHPQYMZQTOCNFJ-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.341	[Ca++]
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Ca+2]

Formula

Name

CALCIUM ION

PDB chain

2o18 Chain C Residue 341 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2o18 Crystal structure of a Thiamine biosynthesis lipoprotein apbE
Resolution	2.2 Å
Binding residue (original residue number in PDB)	T166 D280 D283 T284
Binding residue (residue number reindexed from 1)	T154 D263 D266 T267
Annotation score	1

Enzymatic activity

Enzyme Commision number

2.7.1.180: FAD:protein FMN transferase.

Gene Ontology

	Molecular Function
GO:0016651	oxidoreductase activity, acting on NAD(P)H
GO:0016740	transferase activity
GO:0046872	metal ion binding

	Biological Process
GO:0017013	protein flavinylation

	Cellular Component
GO:0005886	plasma membrane
GO:1990204	oxidoreductase complex

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Molecular Function

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Cellular Component

External links

PDB	RCSB:2o18, PDBe:2o18, PDBj:2o18
PDBsum	2o18
PubMed
UniProt	P0AB85\|APBE_ECOLI FAD:protein FMN transferase (Gene Name=apbE)

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