Structure of PDB 2x0q Chain A

Receptor sequence
>2x0qA (length=582) Species: 518 (Bordetella bronchiseptica) [Search protein sequence]
HPAEIVAHLQPEIWNKVNRLLVRKAISEYAHEWLLEPQRLGPGETPGFER
FRLTLADGAQYDFDAQVMAMRHWRIPPESIVKTVAGVPAPLDALQFVIEI
RDKLGLPVDRLPIYMDEITSTLHGSAYKHGRTTLGAAALARADYQTIETS
MIEGHPSFVANNGRLGFDAEDYHGYAPEAATPVRLMWLAVHKDNAHFSCL
SDMDYDSLMSEELGESAVTDFAARLREQGLHPADYYFMPAHPWQWFNKLS
LAFAPYVAQRKIVCLGYGEEQYLAQQSIRTFFNISRPGKRYVKTSLSILN
MGFMRGLSPYYMAGTPAINEYIHDLISADPWLRANGFRILREVASMGFRN
YYYEAAIDTDTPYKKMFSALWRENPLTLIAPGQNLMTMAALLHVDPQGRA
LLPELIQASGLDAGTWLERYVDAYLTPLIHCFYAHDLVFMPHGENVILVI
QDGVPVRAFMKDIAEESSILNPQVRLPQAAQRLAADVPEAYKLLTIFVDV
FEGYFRHLTQILVETELMPEHDFWRLVAGRIAAYQQAHPQRLDKYRRYDL
FAPDMIHSCLNRLQLANPNLPNPIACFRPSWL
3D structure
PDB2x0q Co-Complex Structure of Alcaligin Biosynthesis Protein C (Alcc) with ATP from Bordetella Bronchiseptica
ChainA
Resolution1.96 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 ATP A G161 H162 Q283 S284 R286 T287 K300 N307 M308 R312 R379 H449 E451 D469 G154 H155 Q276 S277 R279 T280 K293 N300 M301 R305 R372 H442 E444 D462
BS02 MG A D469 E472 E473 D462 E465 E466
BS03 MG A E451 N452 D469 E444 N445 D462
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:2x0q, PDBe:2x0q, PDBj:2x0q
PDBsum2x0q
PubMed
UniProtQ7W557

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