Structure of PDB 3to3 Chain B

Receptor sequence
>3to3B (length=595) Species: 260799 (Bacillus anthracis str. Sterne) [Search protein sequence]
AMDMYHTKILKAIESEDYISVRRRVLRQLVESLIYEGIITPARIEKEEQI
LFLIQGLDEDNKSVTYECYGRERITFGRISIDSLIVRVQDGKQEIQSVAQ
FLEEVFRVVNVEQTKLDSFIHELEQTIFKDTIAQYERCNKSYDELENHLI
DGHPYHPSYKARIGFQYRDNFRYGYEFMRPIKLIWIAAHKKNATVGYENE
VIYDKILKSEVGERKLEAYKERIHSMGCDPKQYLFIPVHPWQWENFIISN
YAEDIQDKGIIYLGESADDYCAQQSMRTLRNVTNPKRPYVKVSLNILNTS
TLRTLKPYSVASAPAISNWLSNVVSQDSYLRDESRVILLKEFSSVMYDTN
KKATYGSLGCIWRESVHHYLGEQEDAVPFNGLYAKEKDGTPIIDAWLNKY
GIENWLRLLIQKAIIPVIHLVVEHGIALESHGQNMILVHKEGLPVRIALK
DFHEGLEFYRPFLKEMNKCPDFTKMHKTYANGKMNDFFEMDRIECLQEMV
LDALFLFNVGELAFVLADKYEWKEESFWMIVVEEIENHFRKYPHLKDRFE
SIQLYTPTFYAEQLTKRRLYIDVESLVHEVPNPLYRARQLNIQKS
3D structure
PDB3to3 Functional and Structural Analysis of the Siderophore Synthetase AsbB through Reconstitution of the Petrobactin Biosynthetic Pathway from Bacillus anthracis.
ChainB
Resolution2.382 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.2.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ATP B G157 H158 S280 R282 K296 R308 N385 Q438 D456 G152 H153 S275 R277 K291 R303 N380 Q433 D451
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016881 acid-amino acid ligase activity
Biological Process
GO:0009058 biosynthetic process
GO:0019290 siderophore biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3to3, PDBe:3to3, PDBj:3to3
PDBsum3to3
PubMed22408253
UniProtQ81RQ8|ASBB_BACAN Citryl-spermidine/3,4-dihydroxybenzoyl-citryl-spermidine:spermidine ligase (Gene Name=asbB)

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