Structure of PDB 6iii Chain A

Receptor sequence
>6iiiA (length=460) Species: 562 (Escherichia coli) [Search protein sequence]
TLSFITRWRDELPATYTTLSPTPLNNARLIWHNAELANTLGIPSSLFKAG
VWGGETLLPGMSPLAQVYSGHQFGVWAGQLGDGRGILLGEQRLADGTTMD
WHLKGAGLTPYSRMGDGRAVLRSTIRESLASEAMHYLGIPTTRALSIVTS
DSPVYRETVEPGAMLMRVAPSHLRFGHFEHFYYRREPEKVRQLADFAIRH
YWSHLADDEDKYRLWFTDVVARTASLIAQWQTVGFAHGVMNTDNMSLLGL
TLDYGPFGFLDDYEPGFICNHSDHQGRYSFDNQPAVALWNLQRLAQTLSP
FVAVDALNEALDSYQQVLLTHYGQRMRQKLGFMTEQKEDNALLNELFSLM
ARERSDYTRTFRMLSLTEQHSAADEFIDRAAFDDWFARYRGRLQQDEVSD
SERQQLMQSVNPALVLRNWLAQRAIEAAEKGDMTELHRLHEALRNPFSDR
DDDYVSRPPD
3D structure
PDB6iii Crystal structure of an uncharacterized protein
ChainA
Resolution2.113 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.108: protein adenylyltransferase.
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 2PN A R87 K107 R170 R177 D256 R84 K104 R167 R174 D253
BS02 AMP A Y71 Q75 G84 G86 R87 S115 R116 G118 D119 G120 D246 N247 Y68 Q72 G81 G83 R84 S112 R113 G115 D116 G117 D243 N244
BS03 MG A N247 D256 N244 D253
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0070733 AMPylase activity
Biological Process
GO:0018117 protein adenylylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6iii, PDBe:6iii, PDBj:6iii
PDBsum6iii
PubMed
UniProtP77649|SELO_ECOLI Protein adenylyltransferase SelO (Gene Name=selO)

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