Structure of PDB 2x3k Chain A

Receptor sequence
>2x3kA (length=575) Species: 556 (Dickeya chrysanthemi) [Search protein sequence]
DVLSRMISEKAALHGLLNCLIKEFAIPEGYLRYEWPDEMKGIPPGAYFDG
ADWKGIPMMIGLPDQLQLFVMVDRRDTFGSQHYLSDVYLRQAGDWQCPDF
EPLVARLLAACEHIAGRKNPELYEQILQSQRLVSAIVSHNGRQRADAPLQ
HYLQSEQGLWFGHPSHPAPKARLWPAHLGQEQWAPEFQARAALHQFEVPV
DGLHIGANGLTPQQVLDGFADQQPASPGHAIICMHPVQAQLFMQDARVQQ
LLRDNVIRDLGQSGRVASPTASIRTWFIDDHDYFIKGSLNVRITNCVRKN
AWYELESTVLIDRLFRQLLDQHADTLGGLVAAAEPGVVSWSPAAAGELDS
HWFREQTGGILRENFCRRTGAERSIMAGTLFARGVDLQPMIQTFLRTHYG
EALDDNALLYWFDDYQTRLLRPVLSLFFNHGVVMEPHLQNSVLVHQQGRP
QQVLLRDFEGVKLTDDLGIRYIDDDIHPRVRQSLLYSREQGWNRIMYCLF
INHLSETILALSQGRPQLAPLMWRRVQQQLRAIQGELKQPSPELDALIAG
HPVACKTNLKVRLAAASYVRLPSPW
3D structure
PDB2x3k Adenylate Forming Enzymes Involved in Nrps-Independent Siderophore Biosynthesis
ChainA
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 A H170 R305 H444 Q446 N509 H163 R298 H437 Q439 N502
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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