Structure of PDB 2x3k Chain B

Receptor sequence
>2x3kB (length=570) Species: 556 (Dickeya chrysanthemi) [Search protein sequence]
DVLSRMISEKAALHGLLNCLIKEFAIPEGYLRYEWPDEMKGIPPGAYFDG
ADWKGIPMMIGLPDQLQLFVMVDRRDTFGSQHYLSDVYLRQGDWQCPDFE
PLVARLLAACEHIAGRKNPELYEQILQSQRLVSAIVSHNGRQRADAPLQH
YLQSEQGLWFGHPSHPAPKARLWPAHLGQEQWAPEFQARAALHQFEVPVD
GLHIGANGLTPQQVLDGFADQQPASPGHAIICMHPVQAQLFMQDARVQQL
LRDNVIRDLGQSGRVASPTASIRTWFIDDHDYFIKGSLNVRITNCVRKNA
WYELESTVLIDRLFRQLLDQHADTLGGLVAAAEPGVVSWSPAAAGELDSH
WFREQTGGILRENFCRRTGAERSIMAGTLFARGVDLQPMIQTFLRTHYGE
ALDDNALLYWFDDYQTRLLRPVLSLFFNHGVVMEPHLQNSVLVHQQGRPQ
QVLLRDFEGVKLTDDLGIRYIHPRVRQSLLYSREQGWNRIMYCLFINHLS
ETILALSQGRPQLAPLMWRRVQQQLRAIQGELKQPSPELDALIAGHPVAC
KTNLKVRLAAASYVRLPSPW
3D structure
PDB2x3k Adenylate Forming Enzymes Involved in Nrps-Independent Siderophore Biosynthesis
ChainB
Resolution2.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 AMP B L166 H170 R305 H444 Q446 N509 L158 H162 R297 H436 Q438 N497
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016881 acid-amino acid ligase activity
GO:0046872 metal ion binding
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:2x3k, PDBe:2x3k, PDBj:2x3k
PDBsum2x3k
PubMed
UniProtQ93AT8

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